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4y2n

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Revision as of 18:04, 26 April 2023

Structure of CFA/I pili major subunit CfaB trimer

Structural highlights

4y2n is a 3 chain structure with sequence from Escherichia coli ETEC H10407. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4y2n"

Categories: Escherichia coli ETEC H10407 | Large Structures | Bao R | Xia D

@@ Line 1: / Line 1: @@
 ==Structure of CFA/I pili major subunit CfaB trimer==
-<StructureSection load='4y2n' size='340' side='right' caption='[[4y2n]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='4y2n' size='340' side='right'caption='[[4y2n]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == 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>
-<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>
 == 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;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 21: @@
 ==See Also==
 *[[Colonization factor antigen|Colonization factor antigen]]
-*[[Pilin|Pilin]]
+*[[Pilin 3D structures|Pilin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </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]]
-[[Category: Structural protein]]

4y2n

From Proteopedia

Revision as of 18:04, 26 April 2023

Structure of CFA/I pili major subunit CfaB trimer

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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