DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA. Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Zhu Y., Hu L., Zhou Y., Yao Q., Liu L., Shao F. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Zhu Y., Hu L., Zhou Y., Yao Q., Liu L., Shao F. DIP original experiment: DIP-216314X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA. Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA. Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Zhu Y., Hu L., Zhou Y., Yao Q., Liu L., Shao F. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Zhu Y., Hu L., Zhou Y., Yao Q., Liu L., Shao F. DIP original experiment: DIP-216317X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA. Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA. Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Zhu Y., Hu L., Zhou Y., Yao Q., Liu L., Shao F. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Zhu Y., Hu L., Zhou Y., Yao Q., Liu L., Shao F. DIP original experiment: DIP-216315X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA. Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA. Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Zhu Y., Hu L., Zhou Y., Yao Q., Liu L., Shao F. Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast pull down pull down predetermined predetermined participant predetermined Zhu Y., Hu L., Zhou Y., Yao Q., Liu L., Shao F. DIP original experiment: DIP-216316X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA. Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA. Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Zhu Y., Hu L., Zhou Y., Yao Q., Liu L., Shao F. Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast pull down pull down predetermined predetermined participant predetermined Zhu Y., Hu L., Zhou Y., Yao Q., Liu L., Shao F. DIP original experiment: DIP-216318X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA. gdib_human Rab GDP dissociation inhibitor beta Guanosine diphosphate dissociation inhibitor 2 GDI2 RABGDIB protein protein human Homo sapiens Human MNEEYDVIVLGTGLTECILSGIMSVNGKKVLHMDRNPYYGGESASITPLEDLYKRFKIPGSPPESMGRGRDWNVDLIPKFLMANGQLVKMLLYTEVTRYLDFKVTEGSFVYKGGKIYKVPSTEAEALASSLMGLFEKRRFRKFLVYVANFDEKDPRTFEGIDPKKTTMRDVYKKFDLGQDVIDFTGHALALYRTDDYLDQPCYETINRIKLYSESLARYGKSPYLYPLYGLGELPQGFARLSAIYGGTYMLNKPIEEIIVQNGKVIGVKSEGEIARCKQLICDPSYVKDRVEKVGQVIRVICILSHPIKNTNDANSCQIIIPQNQVNRKSDIYVCMISFAHNVAAQGKYIAIVSTTVETKEPEKEIRPALELLEPIEQKFVSISDLLVPKDLGTESQIFISRTYDATTHFETTCDDIKNIYKRMTGSEFDFEEMKRKKNDIYGED DIP protein P50395 original sequence version: 92 DIP protein P50395 original sequence version: 137 CE186A2E3A47FCC9 p62820-1 Ras-related protein Rab-1A RAB1A RAB1 YPT1-related protein protein protein human Homo sapiens Human MSSMNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQESFNNVKQWLQEIDRYASENVNKLLVGNKCDLTTKKVVDYTTAKEFADSLGIPFLETSAKNATNVEQSFMTMAAEIKKRMGPGATAGGAEKSNVKIQSTPVKQSGGGCC DIP protein P62820-1 original sequence version: 108 DIP protein P62820-1 original sequence version: 78 drra_legpn Multifunctional virulence effector protein DrrA drrA sidM Defects in Rab1 recruitment protein A protein protein legpn Legionella pneumophila MSIMGRIKMSVNEEQFGSLYSDERDKPLLSPTAQKKFEEYQNKLANLSKIIRENEGNEVSPWQEWENGLRQIYKEMIYDAFDALGVEMPKDMEVHFAGSLAKAQATEYSDLDAFVIVKNDEDIKKVKPVFDALNNLCQRIFTASNQIYPDPIGINPSRLIGTPDDLFGMLKDGMVADVEATAMSILTSKPVLPRYELGEELRDKIKQEPSFSNMVSAKKFYNKAIKDFTAPKEGAEVVSVKTHIMRPIDFMLMGLREEFNLYSEDGAHLSAPGTIRLLREKNLLPEEQIARIESVYNQAMSKRFELHAEHKKEHDEMPYSDAKAMLDEVAKIRELGVQRVTRIENLENAKKLWDNANSMLEKGNISGYLKAANELHKFMKEKNLKEDDLRPELSDKTISPKGYAILQSLWGAASDYSRAAATLTESTVEPGLVSAVNKMSAFFMDCKLSPNERATPDPDFKVGKSKILVGIMQFIKDVADPTSKIWMHNTKALMNHKIAAIQKLERSNNVNDETLESVLSSKGENLSEYLSYKYATKDEGREHRYTASTENFKNVKEKYQQMRGDALKTEILADFKDKLAEATDEQSLKQIVAELKSKDEYRILAKGQGLTTQLLGLKTSSVSSFEKMVEETRESIKSQERQTIKIK DIP protein Q29ST3 original sequence version: 10 gdi2-rab1a-1 4 7 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 6 unspecified role unspecified role bait bait GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast physical association physical association drra-rab1a-7 1 7 unspecified role unspecified role unspecified role unspecified role Region 1-177 Region 1-177 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role Region 193-550 Region 193-550 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction rab1a-gdi2-1 5 7 unspecified role unspecified role bait bait His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 6 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast physical association physical association drra-rab1a-8 3 7 unspecified role unspecified role prey prey ecolx Escherichia coli 8 unspecified role unspecified role bait bait GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Region 193-550 Region 193-550 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction drra-rab1a-9 2 7 unspecified role unspecified role unspecified role unspecified role Region 1-177 Region 1-177 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role Region 193-550 Region 193-550 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction