DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Allosteric mechanism controls traffic in the chaperone/usher pathway. Allosteric mechanism controls traffic in the chaperone/usher pathway. Structure (London, England : 1993) 2012 imex curation Di Yu X., Dubnovitsky A., Pudney AF., Macintyre S., Knight SD., Zavialov AV. 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 Di Yu X., Dubnovitsky A., Pudney AF., Macintyre S., Knight SD., Zavialov AV. DIP original experiment: DIP-251174X Structure (London, England : 1993) 2012 IMEx Allosteric mechanism controls traffic in the chaperone/usher pathway. Allosteric mechanism controls traffic in the chaperone/usher pathway. Allosteric mechanism controls traffic in the chaperone/usher pathway. Structure (London, England : 1993) 2012 imex curation Di Yu X., Dubnovitsky A., Pudney AF., Macintyre S., Knight SD., Zavialov AV. Only protein-protein interactions in vitro In vitro ion exchange chrom ion exchange chromatography IEC IEC ion exchange chrom predetermined predetermined participant predetermined Di Yu X., Dubnovitsky A., Pudney AF., Macintyre S., Knight SD., Zavialov AV. DIP original experiment: DIP-251173X Structure (London, England : 1993) 2012 IMEx Allosteric mechanism controls traffic in the chaperone/usher pathway. Allosteric mechanism controls traffic in the chaperone/usher pathway. Allosteric mechanism controls traffic in the chaperone/usher pathway. Structure (London, England : 1993) 2012 imex curation Di Yu X., Dubnovitsky A., Pudney AF., Macintyre S., Knight SD., Zavialov AV. 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 Di Yu X., Dubnovitsky A., Pudney AF., Macintyre S., Knight SD., Zavialov AV. DIP original experiment: DIP-251175X Structure (London, England : 1993) 2012 IMEx Allosteric mechanism controls traffic in the chaperone/usher pathway. Allosteric mechanism controls traffic in the chaperone/usher pathway. Allosteric mechanism controls traffic in the chaperone/usher pathway. Structure (London, England : 1993) 2012 imex curation Di Yu X., Dubnovitsky A., Pudney AF., Macintyre S., Knight SD., Zavialov AV. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Di Yu X., Dubnovitsky A., Pudney AF., Macintyre S., Knight SD., Zavialov AV. DIP original experiment: DIP-251176X Structure (London, England : 1993) 2012 IMEx Allosteric mechanism controls traffic in the chaperone/usher pathway. caf1_yerpe F1 capsule antigen caf1 YPMT1.84 YP_pMT082 Y1100 protein protein yerpe Yersinia pestis MKKISSVIAIALFGTIATANAADLTASTTATATLVEPARITLTYKEGAPITIMDNGNIDTELLVGTLTLGGYKTGTTSTSVNFTDAAGDPMYLTFTSQDGNNHQFTTKVIGKDSRDFDISPKVNGENLVGDDVVLATGSQDFFVRSIGSKGGKLAAGKYTDAVTVTVSNQ DIP protein P26948 original sequence version: 89 9AC87796A0BA67D9 caf1m_yerpe Chaperone protein caf1M caf1M YPMT1.82 YP_pMT084 Capsule protein fraction 1 Y1098 protein protein yerpe Yersinia pestis MILNRLSTLGIITFGMLSFAANSAQPDIKFASKEYGVTIGESRIIYPLDAAGVMVSVKNTQDYPVLIQSRIYDENKEKESEDPFVVTPPLFRLDAKQQNSLRIAQAGGVFPRDKESLKWLCVKGIPPKDEDIWVDDATNKQKFNPDKDVGVFVQFAINNCIKLLVRPNELKGTPIQFAENLSWKVDGGKLIAENPSPFYMNIGELTFGGKSIPSHYIPPKSTWAFDLPKGLAGARNVSWRIINDQGGLDRLYSKNVTL DIP protein P26926 original sequence version: 104 8049DCC1A80C7391 caf1a_yerpe F1 capsule-anchoring protein caf1A YPMT1.83 Y1099 YP_pMT083 protein protein yerpe Yersinia pestis MRYSKLFLCAGLTLATLPCWGRAYTFDSTMLDTNSGESIDVSLFNQGLQLPGNYFVNVFVNGRKVDSGNIDFRLEKHNGKELLWPCLSSLQLTKYGIDIDKYPDLIKSGTEQCVDLLAIPHSDVQFYFNQQKLSLIVPPQALLPRFDGIMPMQLWDDGIPALFMNYNTNMQTRKFREGGKSLDSYYAQLQPGLNIGAWRFRSSTSWWKQQGWQRSYIYAERGLNTIKSRLTLGETYSDSSIFDSIPIKGIKIASDESMVPYYQWNFAPVVRGIARTQARVEVLRDGYTVSNELVPSGPFELANLPLGGGSGELKVIIHESDGTKQVFTVPYDTPAVALRKGYFEYSMMGGEYRPANDLTQTSYVGALGMKYGLPRNLTLYGGLQGSQNYHAAALGIGAMLGDFGAISTDVTQADSQKNKQKKESGQRWRVRYNKYLQSGTSLNIASEEYATEGFNKLADTLNTYCKPNTRNDCRFDYAKPKNKVQFNLSQSIPGSGTLNFSGYRKNYWRDSRSTTSFSVGYNHFFRNGMSLTLNLSKTQNINKYGEKTSELLSNIWLSFPLSRWLGNNSINSNYQMTSDSHGNTTHEVGVYGEAFDRQLYWDVRERFNEKGRKYTSNALNLNYRGTYGEISGNYSYDQTQSQLGIGVNGNMVITQYGITAGQKTGDTIALVQAPDISGASVGYWPGMKTDFRGYTNYGYLTPYRENKVEINPVTLPNDAEITNNIVSVIPTKGAVVLAKFNARIGGRLFLHLKRSDNKPVPFGSIVTIEGQSSSSGIVGDNSGVYLTGLPKKSKILVKWGRDKNQSCSSNVVLPEKTDISGAYRLSTTCILNN DIP protein P26949 original sequence version: 94 caf1-caf1a-1 2 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role N-terminal domain Region 1-158 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli association association caf1-caf1a-2 3 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role N-terminal domain Region 1-158 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction caf1-caf1a-3 1 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role N-terminal domain Region 1-158 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association caf1-caf1m-1 4 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction