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1l4i
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(New page: 200px<br /><applet load="1l4i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l4i, resolution 2.20Å" /> '''Crystal Structure of...)
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Revision as of 18:07, 20 November 2007
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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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