1l4i
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l4i OCA], [http://www.ebi.ac.uk/pdbsum/1l4i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l4i RCSB]</span> | ||
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[[Category: periplasmic chaperone]] | [[Category: periplasmic chaperone]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:57:55 2008'' |
Revision as of 18:57, 30 March 2008
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| , resolution 2.20Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the Periplasmic Chaperone SfaE
Overview
S pili are sialic acid binding hair-like appendages expressed by pathogenic strains of Escherichia coli. The presence of S pili has been implicated as a virulence factor in both urinary-tract infections and new-born meningitis. Assembly of S pili proceeds via the ubiquitous chaperone/usher pathway. Previously, structures of the homologous chaperones PapD and FimC involved in assembly of P and type-1 pili, respectively, have been solved. Here, the 2.2 A X-ray structure of the S pilus chaperone SfaE is reported. SfaE has the same overall L-shaped structure as PapD and FimC, with two immunoglobulin-like domains oriented at about a 90 degrees angle to each other. Conserved residues in the subunit-binding cleft known to be critical for chaperone function occupy essentially identical positions in SfaE, FimC and PapD. As in free PapD and FimC, the long F1-G1 loop connecting the two last strands of the N-terminal domain is disordered. SfaE crystallizes as a dimer with an extensive dimer interface involving the subunit-binding surfaces of the chaperone. Dimerization via these regions has previously been observed for PapD and might be a general side effect arising from the subunit-binding properties of periplasmic chaperones. The domain interface contains an extended hydrogen-bond network involving three invariant charged residues and two structurally conserved water molecules. It is suggested that disruption of the domain interactions may destabilize the N-terminal domain through exposure of three conserved hydrophobic residues, thereby promoting release of pilus subunits during pilus assembly.
About this Structure
1L4I is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of the S pilus periplasmic chaperone SfaE at 2.2 A resolution., Knight SD, Choudhury D, Hultgren S, Pinkner J, Stojanoff V, Thompson A, Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):1016-22. Epub, 2002 May 29. PMID:12037304
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