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| - | [[Image:1l4i.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1l4i| PDB=1l4i | SCENE= }} | | {{STRUCTURE_1l4i| PDB=1l4i | SCENE= }} |
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| - | '''Crystal Structure of the Periplasmic Chaperone SfaE'''
| + | ===Crystal Structure of the Periplasmic Chaperone SfaE=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12037304}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12037304 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12037304}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Immunoglobulin fold]] | | [[Category: Immunoglobulin fold]] |
| | [[Category: Periplasmic chaperone]] | | [[Category: Periplasmic chaperone]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:32:00 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:41:38 2008'' |
Revision as of 08:41, 2 July 2008
Template:STRUCTURE 1l4i
Crystal Structure of the Periplasmic Chaperone SfaE
Template:ABSTRACT PUBMED 12037304
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
Page seeded by OCA on Wed Jul 2 11:41:38 2008
