1l4i

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[[Image:1l4i.gif|left|200px]]
 
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==Crystal Structure of the Periplasmic Chaperone SfaE==
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The line below this paragraph, containing "STRUCTURE_1l4i", creates the "Structure Box" on the page.
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<StructureSection load='1l4i' size='340' side='right'caption='[[1l4i]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</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>
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<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>
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{{STRUCTURE_1l4i| PDB=1l4i | SCENE= }}
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</table>
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== Function ==
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'''Crystal Structure of the Periplasmic Chaperone SfaE'''
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[https://www.uniprot.org/uniprot/FOCC_ECOLX FOCC_ECOLX] Involved in the biogenesis of the F1C fimbriae.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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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.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l4/1l4i_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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1L4I is a [[Single protein]] structure of sequence from [http://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].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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</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].
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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://www.ncbi.nlm.nih.gov/pubmed/12037304 12037304]
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Choudhury, D.]]
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[[Category: Choudhury D]]
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[[Category: Hultgren, S.]]
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[[Category: Hultgren S]]
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[[Category: Knight, S D.]]
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[[Category: Knight SD]]
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[[Category: Pinkner, J.]]
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[[Category: Pinkner J]]
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[[Category: Stojanoff, V.]]
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[[Category: Stojanoff V]]
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[[Category: Thompson, A.]]
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[[Category: Thompson A]]
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[[Category: Immunoglobulin fold]]
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[[Category: Periplasmic chaperone]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:32:00 2008''
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Current revision

Crystal Structure of the Periplasmic Chaperone SfaE

PDB ID 1l4i

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