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 basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Nature structural & molecular biology 2011 imex curation Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. 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 Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. DIP original experiment: DIP-218479X Nature structural & molecular biology 2011 IMEx Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Nature structural & molecular biology 2011 imex curation Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. 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 Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. DIP original experiment: DIP-218476X Nature structural & molecular biology 2011 IMEx Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Nature structural & molecular biology 2011 imex curation Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. DIP original experiment: DIP-218481X Nature structural & molecular biology 2011 IMEx Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Nature structural & molecular biology 2011 imex curation Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. Only protein-protein interactions ecolx Escherichia coli pull down pull down predetermined predetermined participant predetermined Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. DIP original experiment: DIP-218480X Nature structural & molecular biology 2011 IMEx Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Nature structural & molecular biology 2011 imex curation Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. Only protein-protein interactions in vitro In vitro light scattering light scattering predetermined predetermined participant predetermined Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. DIP original experiment: DIP-218475X Nature structural & molecular biology 2011 IMEx Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Nature structural & molecular biology 2011 imex curation Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. DIP original experiment: DIP-218473X Nature structural & molecular biology 2011 IMEx Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Nature structural & molecular biology 2011 imex curation Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. 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 Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. DIP original experiment: DIP-218477X Nature structural & molecular biology 2011 IMEx Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Nature structural & molecular biology 2011 imex curation Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. DIP original experiment: DIP-218472X Nature structural & molecular biology 2011 IMEx Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Nature structural & molecular biology 2011 imex curation Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. Only protein-protein interactions in vitro In vitro 3d-em 3D electron microscopy 3D-EM electron tomog predetermined predetermined participant predetermined Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. DIP original experiment: DIP-218478X Nature structural & molecular biology 2011 IMEx Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Nature structural & molecular biology 2011 imex curation Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. 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 Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. DIP original experiment: DIP-218474X Nature structural & molecular biology 2011 IMEx Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. rir2_human Ribonucleoside-diphosphate reductase subunit M2 RRM2 RR2 Ribonucleotide reductase small subunit Ribonucleotide reductase small chain protein protein human Homo sapiens Human MLSLRVPLAPITDPQQLQLSPLKGLSLVDKENTPPALSGTRVLASKTARRIFQEPTEPKTKAAAPGVEDEPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARCFYGFQIAMENIHSEMYSLLIDTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIEQEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTNFFEKRVGEYQRMGVMSSPTENSFTLDADF DIP protein P31350 original sequence version: 153 DIP protein P31350 original sequence version: 118 10E6F5F84D34DA94 rir1_yeast Ribonucleoside-diphosphate reductase large chain 1 RNR1 RIR1 Ribonucleotide reductase R1 subunit 1 YER070W CRT7 SDS12 Ribonucleotide reductase large subunit 1 protein protein yeast Saccharomyces cerevisiae Baker's yeast MYVYKRDGRKEPVQFDKITARISRLCYGLDPKHIDAVKVTQRIISGVYEGVTTIELDNLAAETCAYMTTVHPDYATLAARIAISNLHKQTTKQFSKVVEDLYRYVNAATGKPAPMISDDVYNIVMENKDKLNSAIVYDRDFQYSYFGFKTLERSYLLRINGQVAERPQHLIMRVALGIHGRDIEAALETYNLMSLKYFTHASPTLFNAGTPKPQMSSCFLVAMKEDSIEGIYDTLKECALISKTAGGIGLHIHNIRSTGSYIAGTNGTSNGLIPMIRVFNNTARYVDQGGNKRPGAFALYLEPWHADIFDFIDIRKNHGKEEIRARDLFPALWIPDLFMKRVEENGTWTLFSPTSAPGLSDCYGDEFEALYTRYEKEGRGKTIKAQKLWYSILEAQTETGTPFVVYKDACNRKSNQKNLGVIKSSNLCCEIVEYSAPDETAVCNLASVALPAFIETSEDGKTSTYNFKKLHEIAKVVTRNLNRVIDRNYYPVEEARKSNMRHRPIALGVQGLADTFMLLRLPFDSEEARLLNIQIFETIYHASMEASCELAQKDGPYETFQGSPASQGILQFDMWDQKPYGMWDWDTLRKDIMKHGVRNSLTMAPMPTASTSQILGYNECFEPVTSNMYSRRVLSGEFQVVNPYLLRDLVDLGIWDEGMKQYLITQNGSIQGLPNVPQELKDLYKTVWEISQKTIINMAADRSVYIDQSHSLNLFLRAPTMGKLTSMHFYGWKKGLKTGMYYLRTQAASAAIQFTIDQKIADQATENVADISNLKRPSYMPSSASYAASDFVPAAVTANATIPSLDSSSEASREASPAPTGSHSLTKGMAELNVQESKVEVPEVPAPTKNEEKAAPIVDDEETEFDIYNSKVIACAIDNPEACEMCSG 56BE1B077916E419 56BE1B077916E419 rir4_yeast Ribonucleoside-diphosphate reductase small chain 2 RNR4 YGR180C CRT3 Ribonucleotide reductase small subunit 2 Ribonucleotide reductase R2 subunit 2 protein protein yeast Saccharomyces cerevisiae Baker's yeast MEAHNQFLKTFQKERHDMKEAEKDEILLMENSRRFVMFPIKYHEIWAAYKKVEASFWTAEEIELAKDTEDFQKLTDDQKTYIGNLLALSISSDNLVNKYLIENFSAQLQNPEGKSFYGFQIMMENIYSEVYSMMVDAFFKDPKNIPLFKEIANLPEVKHKAAFIERWISNDDSLYAERLVAFAAKEGIFQAGNYASMFWLTDKKIMPGLAMANRNICRDRGAYTDFSCLLFAHLRTKPNPKIIEKIITEAVEIEKEYYSNSLPVEKFGMDLKSIHTYIEFVADGLLQGFGNEKYYNAVNPFEFMEDVATAGKTTFFEKKVSDYQKASDMSKSATPSKEINFDDDF 712853F2D87D3972 712853F2D87D3972 rir2_yeast Ribonucleoside-diphosphate reductase small chain 1 RNR2 YJL026W J1271 CRT6 Ribonucleotide reductase small subunit 1 Ribonucleotide reductase R2 subunit 1 protein protein yeast Saccharomyces cerevisiae Baker's yeast MPKETPSKAAADALSDLEIKDSKSNLNKELETLREENRVKSDMLKEKLSKDAENHKAYLKSHQVHRHKLKEMEKEEPLLNEDKERTVLFPIKYHEIWQAYKRAEASFWTAEEIDLSKDIHDWNNRMNENERFFISRVLAFFAASDGIVNENLVENFSTEVQIPEAKSFYGFQIMIENIHSETYSLLIDTYIKDPKESEFLFNAIHTIPEIGEKAEWALRWIQDADALFGERLVAFASIEGVFFSGSFASIFWLKKRGMMPGLTFSNELICRDEGLHTDFACLLFAHLKNKPDPAIVEKIVTEAVEIEQRYFLDALPVALLGMNADLMNQYVEFVADRLLVAFGNKKYYKVENPFDFMENISLAGKTNFFEKRVSDYQKAGVMSKSTKQEAGAFTFNEDF DB98028408292042 DB98028408292042 rir1_human Ribonucleoside-diphosphate reductase large subunit Ribonucleoside-diphosphate reductase subunit M1 Ribonucleotide reductase large subunit RRM1 RR1 protein protein human Homo sapiens Human MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLAAETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHSPMVAKSTLDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHKEDIDAAIETYNLLSERWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCALISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIYLEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLDEVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNLGTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLNKIIDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGALEASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIAPMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWHEEMKNQIIACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKLTSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKVSKEEEEKERNTAAMVCSLENRDECLMCGS DIP protein P23921 original sequence version: 150 DIP protein P23921 original sequence version: 117 DIP protein P23921 original sequence version: 112 4470A76C61E8F86A rrm1-2 2 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction scrr1-1 8 12 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction scrr1-scrr2-1 1 13 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association scrr1-scrr2-2 3 13 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association rrm1-rrm2-2 7 11 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction scrr1-2 6 12 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction rrm1-3 10 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction scrr2-scrr4-1 4 13 unspecified role unspecified role prey prey ecolx Escherichia coli 14 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 n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli physical association physical association scrr1-scrr2-3 9 13 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association rrm1-4 5 15 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction