4dwh

From Proteopedia

(Difference between revisions)

Revision as of 05:05, 5 August 2016

Structure of the major type 1 pilus subunit FIMA bound to the FIMC (2.5 A resolution)

Structural highlights

4dwh is a 4 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	3sqb
Gene:	b4316, fimC, JW4279 ("Bacillus coli" Migula 1895), b4314, fimA, JW4277, pilA ("Bacillus coli" Migula 1895)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FIMC_ECOLI] Required for the biogenesis of type 1 fimbriae. Binds and interact with FimH. [FIMA1_ECOLI] 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

Type 1 pili from uropathogenic Escherichia coli are filamentous, noncovalent protein complexes mediating bacterial adhesion to the host tissue. All structural pilus subunits are homologous proteins sharing an invariant disulfide bridge. Here we show that disulfide bond formation in the unfolded subunits, catalyzed by the periplasmic oxidoreductase DsbA, is required for subunit recognition by the assembly chaperone FimC and for FimC-catalyzed subunit folding. FimC thus guarantees quantitative disulfide bond formation in each of the up to 3,000 subunits of the pilus. The X-ray structure of the complex between FimC and the main pilus subunit FimA and the kinetics of FimC-catalyzed FimA folding indicate that FimC accelerates folding of pilus subunits by lowering their topological complexity. The kinetic data, together with the measured in vivo concentrations of DsbA and FimC, predict an in vivo half-life of 2 s for oxidative folding of FimA in the periplasm.

Quality control of disulfide bond formation in pilus subunits by the chaperone FimC.,Crespo MD, Puorger C, Scharer MA, Eidam O, Grutter MG, Capitani G, Glockshuber R Nat Chem Biol. 2012 Jul 1. doi: 10.1038/nchembio.1019. PMID:22772153^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Crespo MD, Puorger C, Scharer MA, Eidam O, Grutter MG, Capitani G, Glockshuber R. Quality control of disulfide bond formation in pilus subunits by the chaperone FimC. Nat Chem Biol. 2012 Jul 1. doi: 10.1038/nchembio.1019. PMID:22772153 doi:10.1038/nchembio.1019

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/4dwh"

@@ Line 1: / Line 1: @@
 ==Structure of the major type 1 pilus subunit FIMA bound to the FIMC (2.5 A resolution)==
 <StructureSection load='4dwh' size='340' side='right' caption='[[4dwh]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4dwh]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DWH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DWH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4dwh]] 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=4DWH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DWH FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sqb|3sqb]]</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b4316, fimC, JW4279 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), b4314, fimA, JW4277, pilA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b4316, fimC, JW4279 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), b4314, fimA, JW4277, pilA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=4dwh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dwh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dwh RCSB], [http://www.ebi.ac.uk/pdbsum/4dwh PDBsum]</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=4dwh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dwh OCA], [http://pdbe.org/4dwh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dwh RCSB], [http://www.ebi.ac.uk/pdbsum/4dwh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dwh ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4dwh" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 25: / Line 27: @@
 __TOC__
 </StructureSection>
-[[Category: Escherichia coli]]
+[[Category: Bacillus coli migula 1895]]
 [[Category: Capitani, G]]
 [[Category: Crespo, M]]

4dwh

From Proteopedia

Revision as of 05:05, 5 August 2016

Structure of the major type 1 pilus subunit FIMA bound to the FIMC (2.5 A resolution)

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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