DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ engel-2012-5 in vitro In vitro ampylation assay ampylation assay ampylation assay weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Engel P., Goepfert A., Stanger FV., Harms A., Schmidt A., Schirmer T., Dehio C. DIP original experiment: DIP-252136X Nature 2012 IMEx Adenylylation control by intra- or intermolecular active-site obstruction in Fic proteins. Engel P., Goepfert A., Stanger FV., Harms A., Schmidt A., Schirmer T., Dehio C. Only protein-protein interactions imex curation hartshorne-2009-1 Shewanella oneidensis Shewanella oneidensis molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column western blot western blot Immuno blot Immuno blot Hartshorne RS., Reardon CL., Ross D., Nuester J., Clarke TA., Gates AJ., Mills PC., Fredrickson JK., Zachara JM., Shi L., Beliaev AS., Marshall MJ., Tien M., Brantley S., Butt JN., Richardson DJ. DIP original experiment: DIP-134890X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Characterization of an electron conduit between bacteria and the extracellular environment. Hartshorne RS., Reardon CL., Ross D., Nuester J., Clarke TA., Gates AJ., Mills PC., Fredrickson JK., Zachara JM., Shi L., Beliaev AS., Marshall MJ., Tien M., Brantley S., Butt JN., Richardson DJ. Only protein-protein interactions imex curation hartshorne-2009-2 Shewanella oneidensis Shewanella oneidensis solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Hartshorne RS., Reardon CL., Ross D., Nuester J., Clarke TA., Gates AJ., Mills PC., Fredrickson JK., Zachara JM., Shi L., Beliaev AS., Marshall MJ., Tien M., Brantley S., Butt JN., Richardson DJ. DIP original experiment: DIP-134888X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Characterization of an electron conduit between bacteria and the extracellular environment. Hartshorne RS., Reardon CL., Ross D., Nuester J., Clarke TA., Gates AJ., Mills PC., Fredrickson JK., Zachara JM., Shi L., Beliaev AS., Marshall MJ., Tien M., Brantley S., Butt JN., Richardson DJ. Only protein-protein interactions imex curation hartshorne-2009-3 Shewanella oneidensis Shewanella oneidensis molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column ms participant Identification by mass spectrometry ms participant Hartshorne RS., Reardon CL., Ross D., Nuester J., Clarke TA., Gates AJ., Mills PC., Fredrickson JK., Zachara JM., Shi L., Beliaev AS., Marshall MJ., Tien M., Brantley S., Butt JN., Richardson DJ. DIP original experiment: DIP-134893X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Characterization of an electron conduit between bacteria and the extracellular environment. Hartshorne RS., Reardon CL., Ross D., Nuester J., Clarke TA., Gates AJ., Mills PC., Fredrickson JK., Zachara JM., Shi L., Beliaev AS., Marshall MJ., Tien M., Brantley S., Butt JN., Richardson DJ. Only protein-protein interactions imex curation hartshorne-2009-4 in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Hartshorne RS., Reardon CL., Ross D., Nuester J., Clarke TA., Gates AJ., Mills PC., Fredrickson JK., Zachara JM., Shi L., Beliaev AS., Marshall MJ., Tien M., Brantley S., Butt JN., Richardson DJ. DIP original experiment: DIP-134891X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Characterization of an electron conduit between bacteria and the extracellular environment. Hartshorne RS., Reardon CL., Ross D., Nuester J., Clarke TA., Gates AJ., Mills PC., Fredrickson JK., Zachara JM., Shi L., Beliaev AS., Marshall MJ., Tien M., Brantley S., Butt JN., Richardson DJ. Only protein-protein interactions imex curation hartshorne-2009-5 in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Hartshorne RS., Reardon CL., Ross D., Nuester J., Clarke TA., Gates AJ., Mills PC., Fredrickson JK., Zachara JM., Shi L., Beliaev AS., Marshall MJ., Tien M., Brantley S., Butt JN., Richardson DJ. DIP original experiment: DIP-134889X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Characterization of an electron conduit between bacteria and the extracellular environment. Hartshorne RS., Reardon CL., Ross D., Nuester J., Clarke TA., Gates AJ., Mills PC., Fredrickson JK., Zachara JM., Shi L., Beliaev AS., Marshall MJ., Tien M., Brantley S., Butt JN., Richardson DJ. Only protein-protein interactions imex curation hartshorne-2009-6 Shewanella oneidensis Shewanella oneidensis solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Hartshorne RS., Reardon CL., Ross D., Nuester J., Clarke TA., Gates AJ., Mills PC., Fredrickson JK., Zachara JM., Shi L., Beliaev AS., Marshall MJ., Tien M., Brantley S., Butt JN., Richardson DJ. DIP original experiment: DIP-134892X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Characterization of an electron conduit between bacteria and the extracellular environment. Hartshorne RS., Reardon CL., Ross D., Nuester J., Clarke TA., Gates AJ., Mills PC., Fredrickson JK., Zachara JM., Shi L., Beliaev AS., Marshall MJ., Tien M., Brantley S., Butt JN., Richardson DJ. Only protein-protein interactions imex curation forouhar-2007-2 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Forouhar F., Anderson JL., Mowat CG., Vorobiev SM., Hussain A., Abashidze M., Bruckmann C., Thackray SJ., Seetharaman J., Tucker T., Xiao R., Ma LC., Zhao L., Acton TB., Montelione GT., Chapman SK., Tong L. DIP original experiment: DIP-260551X Proceedings of the National Academy of Sciences of the United States of America 2007 IMEx Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase. Forouhar F., Anderson JL., Mowat CG., Vorobiev SM., Hussain A., Abashidze M., Bruckmann C., Thackray SJ., Seetharaman J., Tucker T., Xiao R., Ma LC., Zhao L., Acton TB., Montelione GT., Chapman SK., Tong L. Only protein-protein interactions imex curation huang-2009-12 ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Huang N., De Ingeniis J., Galeazzi L., Mancini C., Korostelev YD., Rakhmaninova AB., Gelfand MS., Rodionov DA., Raffaelli N., Zhang H. DIP original experiment: DIP-132029X Structure (London, England : 1993) 2009 IMEx Structure and function of an ADP-ribose-dependent transcriptional regulator of NAD metabolism. Huang N., De Ingeniis J., Galeazzi L., Mancini C., Korostelev YD., Rakhmaninova AB., Gelfand MS., Rodionov DA., Raffaelli N., Zhang H. Only protein-protein interactions imex curation huang-2009-13 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Huang N., De Ingeniis J., Galeazzi L., Mancini C., Korostelev YD., Rakhmaninova AB., Gelfand MS., Rodionov DA., Raffaelli N., Zhang H. DIP original experiment: DIP-132030X Structure (London, England : 1993) 2009 IMEx Structure and function of an ADP-ribose-dependent transcriptional regulator of NAD metabolism. Huang N., De Ingeniis J., Galeazzi L., Mancini C., Korostelev YD., Rakhmaninova AB., Gelfand MS., Rodionov DA., Raffaelli N., Zhang H. Only protein-protein interactions imex curation q8e972_sheon kynA SO_4414 protein protein sheon Shewanella oneidensis (strain MR-1) MKPATYNTEAFDEWIRSRFVELNSQLEQLYYQQTDRANVQEVGTELKHTLESEGRELVKALLDEGNTDEGFDSAFDLLGNVGLYMAACRRHEITEPTRETTSPLLEASALAMHIGASIGVTPRFATAHLTTHNRAHNGIYKRFTDLPDEKLFVDYNTKGILAYKRASDALLKIQPLGISHPISHDLLRVTKQALQDVIESNQQLFNRLDTDRFFYCVRPYYKPYRVGSVVYRGANAGDFAGINVIDLTLGLCFANEASYSQMLVDKFLYMMPEDQQILRECMRRPNLMDDFLQAKGCIHQDWYQENLKLFIEVCELHGQTAIQHHNELVTKYIAEPSVSMEQQHLAKVTASGPPLHVLLASLERLRDRRAAVLRDDIRTRYYDLKKLKDSLR o87540_shepu mtrC protein protein shepu shepu Pseudomonas putrefaciens MMNAQKSKIALLLAASAVTMALTGCGGSSGNNGNDGSDGGEPAGSIQTLNLDITKVSYENGAPMVTVFATNEADMPVIGLANLEIKKALQLIPEGATGPGNSANWQGLGSSKSYVDNKNGSYTFKFDAFDSNKVFNAQLTQRFNVVSAAGKLADGTTVPVAEMVEDFDGQGNAPQYTKNIVSHEVCASCHVEGEKIYHQATEVETCISCHTQEFADGRGKPHVAFSHLIHNVHNANKAWGKDNKIPTVAQNIVQDNCQVCHVESDMLTEAKNWSRIPTMEVCSSCHVDIDFAAGKGHSQQLDNSNCIACHNSDWTAELHTAKTTATKNLINQYGIETTSTINTETKAATISVQVVDANGTAVDLKTILPKVQRLEIITNVGPNNATLGYSGKDSIFAIKNGALDPKATINDAGKLVYTTTKDLKLGQNGADSDTAFSFVGWSMCSSEGKFVDCADPAFDGVDVTKYTGMKADLAFATLSGKAPSTRHVDSVNMTACANCHTAEFEIHKGKQHAGFVMTEQLSHTQDANGKAIVGLDACVTCHTPDGTYSFANRGALELKLHKKHVEDAYGLIGGNCASCHSDFNLESFKKKGALNTAAAADKTGLYSTPITATCTTCHTVGSQYMVHTKETLESFGAVVDGTKDDATSAAQSETCFYCHTPTVADHTKVKM E50F612FA9674BE9 q8cvd4_sheon mtrB SO_1776 protein protein sheon Shewanella oneidensis (strain MR-1) MKFKLNLITLALLANTGLAVAADGYGLANANTEKVKLSAWSCKGCVVETGTSGTVGVGVGYNSEEDIRSANAFGTSNEVAGKFDADLNFKGEKGYRASVDAYQLGMDGGRLDVNAGKQGQYNVNVNYRQIATYDSNSALSPYAGIGGNNLTLPDNWITAGSSNQMPLLMDSLNALELSLKRERTGLGFEYQGESLWSTYVNYMREEKTGLKQASGSFFNQSMMLAEPVDYTTDTIEAGVKLKGDRWFTALSYNGSIFKNEYNQLDFENAFNPTFGAQTQGTMALDPDNQSHTVSLMGQYNDGSNALSGRILTGQMSQDQALVTDNYRYANQLNTDAVDAKVDLLGMNLKVVSKVSNDLRLTGSYDYYDRDNNTQVEEWTQISINNVNGKVAYNTPYDNRTQRFKVAADYRITRDIKLDGGYDFKRDQRDYQDRETTDENTVWARLRVNSFDTWDMWVKGSYGNRDGSQYQASEWTSSETNSLLRKYNLADRDRTQVEARITHSPLESLTIDVGARYALDDYTDTVIGLTESKDTSYDANISYMITADLLATAFYNYQTIESEQAGSSNYSTPTWTGFIEDQVDVVGAGISYNNLLENKLRLGLDYTYSNSDSNTQVRQGITGDYGDYFAKVHNINLYAQYQATEKLALRFDYKIENYKDNDAANDIAVDGIWNVVGFGSNSHDYTAQMLMLSMSYKL BF630F6A80E7CA22 q8eg35_sheon mtrA SO_1777 protein protein sheon Shewanella oneidensis (strain MR-1) MKNCLKMKNLLPALTITMAMSAVMALVVTPNAYASKWDEKMTPEQVEATLDKKFAEGNYSPKGADSCLMCHKKSEKVMDLFKGVHGAIDSSKSPMAGLQCEACHGPLGQHNKGGNEPMITFGKQSTLSADKQNSVCMSCHQDDKRMSWNGGHHDNADVACASCHQVHVAKDPVLSKNTEMEVCTSCHTKQKADMNKRSSHPLKWAQMTCSDCHNPHGSMTDSDLNKPSVNDTCYSCHAEKRGPKLWEHAPVTENCVTCHNPHGSVNDGMLKTRAPQLCQQCHASDGHASNAYLGNTGLGSNVGDNAFTGGRSCLNCHSQVHGSNHPSGKLLQR 72F75E3532B8E847 sofic_sheon Protein adenylyltransferase SoFic fic AMPylator SoFic SO_4266 protein protein sheon Shewanella oneidensis (strain MR-1) MEWQAEQAYNHLPPLPLDSKLAELAETLPILKACIPARAALAELKQAGELLPNQGLLINLLPLLEAQGSSEIENIVTTTDKLFQYAQEDSQADPMTKEALRYRTALYQGFTQLSNRPLCVTTALEICSTIKSVQMDVRKVPGTSLTNQATGEVIYTPPAGESVIRDLLSNWEAFLHNQDDVDPLIKMAMAHYQFEAIHPFIDGNGRTGRVLNILYLIDQQLLSAPILYLSRYIVAHKQDYYRLLLNVTTQQEWQPWIIFILNAVEQTAKWTTHKIAAARELIAHTTEYVRQQLPKIYSHELVQVIFEQPYCRIQNLVESGLAKRQTASVYLKQLCDIGVLEEVQSGKEKLFVHPKFVTLMTKDSNQFSRYAL q8efj3_sheon nrtR SO_1979 protein protein sheon Shewanella oneidensis (strain MR-1) MTEAEYLANYDPKAFKAQLLTVDAVLFTYHDQQLKVLLVQRSNHPFLGLWGLPGGFIDETCDESLEQTVLRKLAEKTAVVPPYIEQLCTVGNNSRDARGWSVTVCYTALMSYQACQIQIASVSDVKWWPLADVLQMPLAFDHLQLIEQARERLTQKALYSLVPGFALSEPFTLPELQHVHEVLLGKPIQGKSFRRRVEQADLLIDTGLKRTERGRPANLYCLKPDTASYRFLRNLEC CF6B2B3914AB10CD fic-1 3235672 N/A 3235680 putative self putative self unspecified role unspecified role Q8E9K5:p.Glu73Gly E73G mutation increasing rate mutation increasing interaction rate mutation increasing rate substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli ampylation ampylation reaction ampylation false false false mtra-mtrb-1 3201219 N/A 3201225 unspecified role unspecified role unspecified role unspecified role Shewanella oneidensis Shewanella oneidensis N/A 3201226 unspecified role unspecified role unspecified role unspecified role Shewanella oneidensis Shewanella oneidensis N/A 3201227 unspecified role unspecified role unspecified role unspecified role Shewanella oneidensis Shewanella oneidensis physical association physical association false false false mtra-mtrb-2 3201220 N/A 3201225 unspecified role unspecified role unspecified role unspecified role Shewanella oneidensis Shewanella oneidensis N/A 3201226 unspecified role unspecified role unspecified role unspecified role Shewanella oneidensis Shewanella oneidensis N/A 3201227 unspecified role unspecified role unspecified role unspecified role Shewanella oneidensis Shewanella oneidensis physical association physical association false false false mtra-mtrb-3 3201221 N/A 3201226 unspecified role unspecified role unspecified role unspecified role Shewanella oneidensis Shewanella oneidensis N/A 3201227 unspecified role unspecified role unspecified role unspecified role Shewanella oneidensis Shewanella oneidensis direct interaction direct interaction false false false mtra-mtrc-1 3201222 N/A 3201225 unspecified role unspecified role unspecified role unspecified role Shewanella oneidensis Shewanella oneidensis N/A 3201227 unspecified role unspecified role unspecified role unspecified role Shewanella oneidensis Shewanella oneidensis direct interaction direct interaction false false false mtra-mtrb-4 3201223 N/A 3201225 unspecified role unspecified role unspecified role unspecified role Shewanella oneidensis Shewanella oneidensis N/A 3201226 unspecified role unspecified role unspecified role unspecified role Shewanella oneidensis Shewanella oneidensis N/A 3201227 unspecified role unspecified role unspecified role unspecified role Shewanella oneidensis Shewanella oneidensis physical association physical association false false false mtra-mtrb-5 3201224 N/A 3201226 unspecified role unspecified role unspecified role unspecified role Shewanella oneidensis Shewanella oneidensis N/A 3201227 unspecified role unspecified role unspecified role unspecified role Shewanella oneidensis Shewanella oneidensis direct interaction direct interaction false false false kyna-2 3151805 N/A 3151807 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false sonrtr-1 3193954 N/A 3193956 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false sonrtr-2 3193955 N/A 3193956 unspecified role unspecified role unspecified role unspecified role Region 1-159 Region 1-159 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint guettou-2013-3 Structural insights into substrate recognition in proton-dependent oligopeptide transporters. in vitro In vitro crosslink cross-linking study crosslink weight by staining molecular weight estimation by staining weight by staining Guettou F., Quistgaard E.M., Trésaugues L., Moberg P., Jegerschöld C., Zhu L., Jong A.J., Nordlund P., Löw C. par.nordlund@ki.se EMBO Rep. (1469-221X) 2013 Only protein-protein interactions imex curation guettou-2013-4 Structural insights into substrate recognition in proton-dependent oligopeptide transporters. in vitro In vitro bn-page blue native page bn-page weight by staining molecular weight estimation by staining weight by staining Guettou F., Quistgaard E.M., Trésaugues L., Moberg P., Jegerschöld C., Zhu L., Jong A.J., Nordlund P., Löw C. par.nordlund@ki.se EMBO Rep. (1469-221X) 2013 Only protein-protein interactions imex curation guettou-2013-1 Structural insights into substrate recognition in proton-dependent oligopeptide transporters. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Guettou F., Quistgaard E.M., Trésaugues L., Moberg P., Jegerschöld C., Zhu L., Jong A.J., Nordlund P., Löw C. par.nordlund@ki.se EMBO Rep. (1469-221X) 2013 Only protein-protein interactions imex curation guettou-2013-2 Structural insights into substrate recognition in proton-dependent oligopeptide transporters. in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Guettou F., Quistgaard E.M., Trésaugues L., Moberg P., Jegerschöld C., Zhu L., Jong A.J., Nordlund P., Löw C. par.nordlund@ki.se EMBO Rep. (1469-221X) 2013 Only protein-protein interactions imex curation guettou-2013-5 Structural insights into substrate recognition in proton-dependent oligopeptide transporters. in vitro In vitro electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy predetermined predetermined participant predetermined Guettou F., Quistgaard E.M., Trésaugues L., Moberg P., Jegerschöld C., Zhu L., Jong A.J., Nordlund P., Löw C. par.nordlund@ki.se EMBO Rep. (1469-221X) 2013 Only protein-protein interactions imex curation anonymous-2014f-1 The X-ray crystal structure of Shewanella oneidensis OmcA reveals new insight at the microbemineral interface in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined d.richardson@uea.ac.uk 2014 imex curation Edwards M.J., Baiden N., Johs A., Tomanicek S.J., Liang L., Shi L., Fredrickson J.K., Zachara J.M., Gates A.J., Butt J.N., Richardson D.J., Clarke T.A. FEBS Lett. (0014-5793) Only protein-protein interactions q8ehe6_sheon SO_1277 protein protein sheon Shewanella oneidensis (strain MR-1) MTLGTNQVSKTHSFMTVSLIELWERFGYYGMQALIVYFMVQRLGFDDSRANLVWSACAALIYVSPAIGGWVGDKILGTKRTMLLGAGILSVGYALMTVPTENTWFMFSALGVIVVGNGLFKPNAGNLVRKIYEGDDSKIDSAFTIYYMAVNVGSTFSMLLTPWIKDYVNAQYGNEFGWHAAFAVCCVGILVGLGNYALMHKSLANYGSEPDTRPVNKKSLAIVLALAALSVVASAIILEYEDVARVFVYAAGVAVLGIFFHLIRTSEPSERAGLIAALILTVQTVFFFIFYQQMSTSLALFALRNVDWDFQVFGTHLWTWSPAQFQALNPIWIMVLSPVLAWSYSWAGRNNKDFSIAAKFALGFAVVAIGFFIYGFAGQFAVNGKTSSWVMIWGYASYSLGELLVSGLGLAMIARYVPARMGGFMMGAYFVASGISQYLGGVVANFASVPQDLVDPLQTLPVYTNLFNKLGVAAVVCTIIALAVLPLMRRLTESHHAHSSIENNAAASLRDVKAEQ q5m4h8_strt2 dtpT stu0970 protein protein strt2 Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311) MEDKGKTFFGQPLGLSTLFMTEMWERFSYYGMRAILLYYMWFLISTGDLHITRATAASIMAIYASMVYLSGTIGGFVADRIIGARPAVFWGGVLIMLGHIVLALPFGASALFGSIILIIIGTGFLKPNVSTLVGTLYDEHDRRRDAGFSIFVFGINLGAFIAPLIVGAAQEAAGYHVAFSLAAIGMFIGLLVYYFGGKKTLDPHYLRPTDPLAPEEVKPLLVKVSLAVAGFIAIIVVMNLVGWNSLPAYINLLTIVAIAIPVFYFAWMISSVKVTSTEHLRVVSYIPLFIAAVLFWAIEEQGSVVLATFAAERVDSSWFPVSWFQSLNPLFIMLYTPFFAWLWTAWKKNQPSSPTKFAVGLMFAGLSFLLMAIPGALYGTSGKVSPLWLVGSWALVILGEMLISPVGLSVTTKLAPKAFNSQMMSMWFLSSSVGSALNAQLVTLYNAKSEVAYFSYFGLGSVVLGIVLVFLSKRIQGLMQGVE q8eg33_sheon omcA SO_1779 protein protein sheon Shewanella oneidensis (strain MR-1) MMKRFNFNTATKAMLGAGLLSLLLTGCGGSDGKDGEDGKPGVVGVNINSTSTLKAKFTNATVDAGKVTVNFTLENANGVAVLGLTKDHDLRFGIAQLTPVKEKVGETEADRGYQWQAYINAKKEPGTVPSGVDNLNPSTQFQANVESANKCDTCLVDHGDGSYSYTYQVNVANVTEPVKVTYSADATQRATMELELPQLAANAHFDWQPSTGKTEGIQTRNVVSIQACYTCHQPESLALHGGRRIDIENCASCHTATSGDPESGNSIEFTYMIHAIHKGGERHTFDATGAQVPAPYKIIGYGGKVIDYGKVHYPQKPAADCAACHVEGAGAPANADLFKADLSNQACIGCHTEKPSAHHSSTDCMACHNATKPYGGTGSAAKRHGDVMKAYNDSLGYKAKFSNIGIKNNALTFDVQILDNKDQPIGKEFISDPSAYTKSSIYFSWGIDKDYPAYTAGSRYSDRGFALSNSKVSTYNEATKTFTIDSTNSNLKLPADLTGMNVELYAGVATCFNKGGYGVEDVVATPCSTDTRYAYIQDQPFRFKWNGTDTNSAAEKRRAIIDTAKCSGCHNKEIVHYDNGVNCQACHTPDKGLKTDNTYPGTKVPTSFAWKAHESEGHYLKYAGVQSGTVLKTDCATCHTADKSNVVTGIALGRSPERAWLYGDIKNNGAVIWVSSDAGACLSCHQKYLSDAAKSHIETNGGILNGTSAADVQTRASESCATCHTPSQLMEAHGN q8ehe6-1 1459453 n/a 1459458 weight by staining molecular weight estimation by staining weight by staining unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction false false false f4b q8ehe6-1 1459453 n/a 1459458 weight by staining molecular weight estimation by staining weight by staining unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 3.0 direct interaction direct interaction false false false f4b q8ehe6-1 1459453 n/a 1459458 weight by staining molecular weight estimation by staining weight by staining unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction false false false f4b dtpt 1459453 n/a 1459459 weight by staining molecular weight estimation by staining weight by staining unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction false false false f4b q8ehe6-1 1459454 n/a 1459458 weight by staining molecular weight estimation by staining weight by staining unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction false false false f4c dtpt-1 1459454 n/a 1459459 weight by staining molecular weight estimation by staining weight by staining unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction false false false f4c q8ehe6 1459455 n/a 1459458 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction false false false f1a f2a f2b f2c st1 sf6 sf7 The crystal form used for the structure determination of PepTSo2 is in a dimeric conformation. This dimer interface appears to be stabilized by the presence of a zinc ion and is most likely a crystal-packing artefact (supplementary Figs 6 and 7 online). However, a second crystal form of PepTSo2 in spacegroup P3121, diffracting to 4.6A° resolution, was obtained in a crystallization condition in the absence of zinc, and molecular replacement into this form did indeed show a tetrameric assembly in the crystal lattice, which might correspond to the tetramer visible in the EM experiments (Fig 4E). Both structures mainly differ in the position of TM12, which mediates key interactions in the oligomeric assembly (Fig 4E,F). Higher resolution data of this crystal form and more functional data will be necessary to unravel potential structural differences of transporter units within the tetramer and the relevance of the oligomerization q8ehe6-q8ehe6 1459456 n/a 1459458 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified n/a 1459458 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction false false false f4a While screening various POTs for structural studies, we realized that PepTSo2 elutes after significantly shorter retention times on an analytical gel filtration column compared to previously characterized POTs (Fig 4A), indicative of a higher oligomer assembly. q8ehe6-1 1459457 n/a 1459458 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction false false false f4d f4e f4f omca 1533529 n/a OmcA 1533530 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction false false false t1 f1 f2 sf3 sf4 sf5 The crystal structure of OmcA reveals four molecules in the asymmetric unit giving a solvent content of 73% (Fig. S3). Superposition of the four OmcA molecules revealed that the overall RMSD between the main-chain atoms of each monomer were less than 0.5 Å, indicating no significant structural differences between the monomers of the asymmetric unit. Analysis of the arrangement of the four OmcA molecules in the asymmetric unit reveals two different orientations where the four monomers can be arranged in two structurally conserved OmcA dimers (Fig. S4).