|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of the FimD usher traversed by the pilus tip complex assembly composed of FimC:FimF:FimG:FimH== | | ==Crystal structure of the FimD usher traversed by the pilus tip complex assembly composed of FimC:FimF:FimG:FimH== |
| - | <StructureSection load='4j3o' size='340' side='right' caption='[[4j3o]], [[Resolution|resolution]] 3.80Å' scene=''> | + | <StructureSection load='4j3o' size='340' side='right'caption='[[4j3o]], [[Resolution|resolution]] 3.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4j3o]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J3O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J3O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4j3o]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J3O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J3O FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fimG, b4319, JW4282 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), fimH, b4320, JW4283 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), fimC, b4316, JW4279 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), fimF, b4318, JW4281 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), fimD, b4317, JW5780 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | </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=4j3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j3o OCA], [https://pdbe.org/4j3o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j3o RCSB], [https://www.ebi.ac.uk/pdbsum/4j3o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j3o ProSAT]</span></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=4j3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j3o OCA], [http://pdbe.org/4j3o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j3o RCSB], [http://www.ebi.ac.uk/pdbsum/4j3o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j3o ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FIMF_ECOLI FIMF_ECOLI]] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Involved in the integration of FimH in the fimbriae. [[http://www.uniprot.org/uniprot/FIMG_ECOLI FIMG_ECOLI]] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Involved in the integration of FimH in the fimbriae. [[http://www.uniprot.org/uniprot/FIMC_ECOLI FIMC_ECOLI]] Required for the biogenesis of type 1 fimbriae. Binds and interact with FimH. [[http://www.uniprot.org/uniprot/FIMH_ECOLI FIMH_ECOLI]] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed. [[http://www.uniprot.org/uniprot/FIMD_ECOLI FIMD_ECOLI]] Involved in the export and assembly of FimA fimbrial subunits across the outer membrane. | + | [https://www.uniprot.org/uniprot/FIMG_ECOLI FIMG_ECOLI] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Involved in the integration of FimH in the fimbriae. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 18: |
Line 17: |
| | </div> | | </div> |
| | <div class="pdbe-citations 4j3o" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4j3o" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Adhesin 3D structures|Adhesin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Geibel, S]]
| + | [[Category: Large Structures]] |
| - | [[Category: Waksman, G]]
| + | [[Category: Geibel S]] |
| - | [[Category: Adhesion]]
| + | [[Category: Waksman G]] |
| - | [[Category: Bacterial outer membrane]]
| + | |
| - | [[Category: Beta barrel]]
| + | |
| - | [[Category: Cell adhesion-chaperone-membrane protein complex]]
| + | |
| - | [[Category: D-mannose-binding]] | + | |
| - | [[Category: Immunglobuline-like fold]] | + | |
| - | [[Category: Pilus subunit translocation]] | + | |
| - | [[Category: Type 1 pilus assembly]]
| + | |
| Structural highlights
Function
FIMG_ECOLI Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Involved in the integration of FimH in the fimbriae.
Publication Abstract from PubMed
Type 1 pili, produced by uropathogenic Escherichia coli, are multisubunit fibres crucial in recognition of and adhesion to host tissues. During pilus biogenesis, subunits are recruited to an outer membrane assembly platform, the FimD usher, which catalyses their polymerization and mediates pilus secretion. The recent determination of the crystal structure of an initiation complex provided insight into the initiation step of pilus biogenesis resulting in pore activation, but very little is known about the elongation steps that follow. Here, to address this question, we determine the structure of an elongation complex in which the tip complex assembly composed of FimC, FimF, FimG and FimH passes through FimD. This structure demonstrates the conformational changes required to prevent backsliding of the nascent pilus through the FimD pore and also reveals unexpected properties of the usher pore. We show that the circular binding interface between the pore lumen and the folded substrate participates in transport by defining a low-energy pathway along which the nascent pilus polymer is guided during secretion.
Structural and energetic basis of folded-protein transport by the FimD usher.,Geibel S, Procko E, Hultgren SJ, Baker D, Waksman G Nature. 2013 Apr 11;496(7444):243-6. doi: 10.1038/nature12007. PMID:23579681[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Geibel S, Procko E, Hultgren SJ, Baker D, Waksman G. Structural and energetic basis of folded-protein transport by the FimD usher. Nature. 2013 Apr 11;496(7444):243-6. doi: 10.1038/nature12007. PMID:23579681 doi:http://dx.doi.org/10.1038/nature12007
|
