4dwh: Difference between revisions

Revision as of 08:41, 21 September 2022

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 Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	PEG, PG4, PGE, PO4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

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

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OCA

[1] 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]

@@ 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=''>
+<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/"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>
+<table><tr><td colspan='2'>[[4dwh]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/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>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4dwh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dwh OCA], [https://pdbe.org/4dwh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dwh RCSB], [https://www.ebi.ac.uk/pdbsum/4dwh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dwh ProSAT]</span></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://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 ==
-[[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/FIMA1_ECOLI 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.
+[[https://www.uniprot.org/uniprot/FIMC_ECOLI FIMC_ECOLI]] Required for the biogenesis of type 1 fimbriae. Binds and interact with FimH.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 18: @@
 </div>
 <div class="pdbe-citations 4dwh" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Pilin 3D structures|Pilin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
-[[Category: Capitani, G]]
+[[Category: Large Structures]]
-[[Category: Crespo, M]]
+[[Category: Capitani G]]
-[[Category: Glockshuber, R]]
+[[Category: Crespo M]]
-[[Category: Puorger, C]]
+[[Category: Glockshuber R]]
-[[Category: Scharer, M A]]
+[[Category: Puorger C]]
-[[Category: Immunoglobin-like fold]]
+[[Category: Scharer MA]]
-[[Category: Involved in type 1 pilus assembly]]
-[[Category: Protein-chaperone complex]]
-[[Category: Structural protein-chaperone complex]]

4dwh: Difference between revisions

Revision as of 08:41, 21 September 2022

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

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