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| <StructureSection load='6k73' size='340' side='right'caption='[[6k73]], [[Resolution|resolution]] 2.77Å' scene=''> | | <StructureSection load='6k73' size='340' side='right'caption='[[6k73]], [[Resolution|resolution]] 2.77Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6k73]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K73 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6K73 FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K73 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K73 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7742Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">D4V05_24280 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), cfaE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6k73 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k73 OCA], [http://pdbe.org/6k73 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k73 RCSB], [http://www.ebi.ac.uk/pdbsum/6k73 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k73 ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6k73 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k73 OCA], [https://pdbe.org/6k73 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k73 RCSB], [https://www.ebi.ac.uk/pdbsum/6k73 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k73 ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| |
| == Publication Abstract from PubMed ==
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| Colonization factor CFA/I defines the major adhesive fimbriae of enterotoxigenic Escherichia coli and mediates bacterial attachment to host intestinal epithelial cells. The CFA/I fimbria consists of a tip-localized minor adhesive subunit, CfaE, and thousands of copies of the major subunit CfaB polymerized into an ordered helical rod. Biosynthesis of CFA/I fimbriae requires the assistance of the periplasmic chaperone CfaA and outer membrane usher CfaC. Although the CfaE subunit is proposed to initiate the assembly of CFA/I fimbriae, how it performs this function remains elusive. Here, we report the establishment of an in vitro assay for CFA/I fimbria assembly and show that stabilized CfaA-CfaB and CfaA-CfaE binary complexes together with CfaC are sufficient to drive fimbria formation. The presence of both CfaA-CfaE and CfaC accelerates fimbria formation, while the absence of either component leads to linearized CfaB polymers in vitro. We further report the crystal structure of the stabilized CfaA-CfaE complex, revealing features unique for biogenesis of Class 5 fimbriae.
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| Chaperone-tip adhesin complex is vital for synergistic activation of CFA/I fimbriae biogenesis.,He LH, Wang H, Liu Y, Kang M, Li T, Li CC, Tong AP, Zhu YB, Song YJ, Savarino SJ, Prouty MG, Xia D, Bao R PLoS Pathog. 2020 Oct 2;16(10):e1008848. doi: 10.1371/journal.ppat.1008848., eCollection 2020 Oct. PMID:33007034<ref>PMID:33007034</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6k73" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Bacillus coli migula 1895]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Bao, R]] | | [[Category: Bao R]] |
| [[Category: He, L H]] | | [[Category: He LH]] |
| [[Category: Adhesive subunit]]
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| [[Category: Binding motif]]
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| [[Category: Chaperone]]
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| [[Category: Chaperone-usher fimbriae]]
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| [[Category: Enterotoxigenic escherichia coli]]
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| [[Category: Periplasmic chaperone]]
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