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| ==Structure of CFA/I pili major subunit CfaB trimer== | | ==Structure of CFA/I pili major subunit CfaB trimer== |
- | <StructureSection load='4y2n' size='340' side='right' caption='[[4y2n]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='4y2n' size='340' side='right'caption='[[4y2n]], [[Resolution|resolution]] 2.40Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4y2n]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoh1 Ecoh1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y2N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y2N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4y2n]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_ETEC_H10407 Escherichia coli ETEC H10407]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y2N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y2N FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4y2l|4y2l]], [[4y2o|4y2o]]</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=4y2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y2n OCA], [https://pdbe.org/4y2n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y2n RCSB], [https://www.ebi.ac.uk/pdbsum/4y2n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y2n ProSAT]</span></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cfaB, ETEC_p948_0400 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=316401 ECOH1])</td></tr>
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- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4y2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y2n OCA], [http://pdbe.org/4y2n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y2n RCSB], [http://www.ebi.ac.uk/pdbsum/4y2n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y2n ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/FMC1_ECOH1 FMC1_ECOH1]] Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs. | + | [https://www.uniprot.org/uniprot/FMC1_ECOH1 FMC1_ECOH1] Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs. |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| ==See Also== | | ==See Also== |
| *[[Colonization factor antigen|Colonization factor antigen]] | | *[[Colonization factor antigen|Colonization factor antigen]] |
- | *[[Pilin|Pilin]] | + | *[[Pilin 3D structures|Pilin 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Ecoh1]] | + | [[Category: Escherichia coli ETEC H10407]] |
- | [[Category: Bao, R]]
| + | [[Category: Large Structures]] |
- | [[Category: Xia, D]]
| + | [[Category: Bao R]] |
- | [[Category: Enterotoxigenic escherichia coli]]
| + | [[Category: Xia D]] |
- | [[Category: Fimbriae]] | + | |
- | [[Category: Major pilin]] | + | |
- | [[Category: Periplasmic chaperone]] | + | |
- | [[Category: Self-assembly]]
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- | [[Category: Structural protein]]
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| Structural highlights
Function
FMC1_ECOH1 Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs.
Publication Abstract from PubMed
The assembly of the class 5 colonization factor antigen I (CFA/I) fimbriae of enterotoxigenic E. coli was proposed to proceed via the alternate chaperone-usher pathway. Here, we show that in the absence of the chaperone CfaA, CfaB, the major pilin subunit of CFA/I fimbriae, is able to spontaneously refold and polymerize into cyclic trimers. CfaA kinetically traps CfaB to form a metastable complex that can be stabilized by mutations. Crystal structure of the stabilized complex reveals distinctive interactions provided by CfaA to trap CfaB in an assembly competent state through donor-strand complementation (DSC) and cleft-mediated anchorage. Mutagenesis indicated that DSC controls the stability of the chaperone-subunit complex and the cleft-mediated anchorage of the subunit C-terminus additionally assist in subunit refolding. Surprisingly, over-stabilization of the chaperone-subunit complex led to delayed fimbria assembly, whereas destabilizing the complex resulted in no fimbriation. Thus, CfaA acts predominantly as a kinetic trap by stabilizing subunit to avoid its off-pathway self-polymerization that results in energetically favorable trimers and could serve as a driving force for CFA/I pilus assembly, representing an energetic landscape unique to class 5 fimbria assembly.
Off-pathway assembly of fimbria subunits is prevented by chaperone CfaA of CFA/I fimbriae from enterotoxigenic E. coli.,Bao R, Liu Y, Savarino SJ, Xia D Mol Microbiol. 2016 Dec;102(6):975-991. doi: 10.1111/mmi.13530. Epub 2016 Oct 7. PMID:27627030[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bao R, Liu Y, Savarino SJ, Xia D. Off-pathway assembly of fimbria subunits is prevented by chaperone CfaA of CFA/I fimbriae from enterotoxigenic E. coli. Mol Microbiol. 2016 Dec;102(6):975-991. doi: 10.1111/mmi.13530. Epub 2016 Oct 7. PMID:27627030 doi:http://dx.doi.org/10.1111/mmi.13530
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