1l4i

<table><tr><td colspan='2'>[[1l4i]] is a 2 chain structure with sequence from [https://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=1L4I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L4I FirstGlance]. <br>

</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=1l4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l4i OCA], [https://pdbe.org/1l4i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l4i RCSB], [https://www.ebi.ac.uk/pdbsum/1l4i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l4i ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/FOCC_ECOLX FOCC_ECOLX]] Involved in the biogenesis of the F1C fimbriae.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:12037304</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: Choudhury, D]]

[[Category: Hultgren, S]]

[[Category: Knight, S D]]

[[Category: Pinkner, J]]

[[Category: Stojanoff, V]]

[[Category: Thompson, A]]

[[Category: Periplasmic chaperone]]