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New page: left|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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[[Image:1l4i.gif|left|200px]]<br /><applet load="1l4i" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1l4i, resolution 2.20&Aring;" />
'''Crystal Structure of the Periplasmic Chaperone SfaE'''<br />


==Overview==
==Crystal Structure of the Periplasmic Chaperone SfaE==
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.
<StructureSection load='1l4i' size='340' side='right'caption='[[1l4i]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1l4i]] is a 2 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=1L4I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L4I FirstGlance]. <br>
1L4I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L4I OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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>
==Reference==
</table>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12037304 12037304]
== Function ==
[https://www.uniprot.org/uniprot/FOCC_ECOLX FOCC_ECOLX] Involved in the biogenesis of the F1C fimbriae.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l4/1l4i_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1l4i ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Choudhury, D.]]
[[Category: Choudhury D]]
[[Category: Hultgren, S.]]
[[Category: Hultgren S]]
[[Category: Knight, S.D.]]
[[Category: Knight SD]]
[[Category: Pinkner, J.]]
[[Category: Pinkner J]]
[[Category: Stojanoff, V.]]
[[Category: Stojanoff V]]
[[Category: Thompson, A.]]
[[Category: Thompson A]]
[[Category: immunoglobulin fold]]
[[Category: periplasmic chaperone]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:15:09 2007''
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