4bwr

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<StructureSection load='4bwr' size='340' side='right'caption='[[4bwr]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
<StructureSection load='4bwr' size='340' side='right'caption='[[4bwr]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4bwr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecol6 Ecol6]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2xm6 2xm6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BWR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BWR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4bwr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_CFT073 Escherichia coli CFT073]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2xm6 2xm6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BWR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BWR FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4bwr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bwr OCA], [https://pdbe.org/4bwr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bwr RCSB], [https://www.ebi.ac.uk/pdbsum/4bwr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bwr ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4bwr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bwr OCA], [http://pdbe.org/4bwr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bwr RCSB], [http://www.ebi.ac.uk/pdbsum/4bwr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bwr ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[[https://www.uniprot.org/uniprot/ESIB_ECOL6 ESIB_ECOL6]] Upon host (human neutrophil) infection interferes with productive FCAR signaling, inhibiting secreted IgA (SIgA) effector functions and probably avoiding neutrophil activation. Inhibits the SIgA-mediated oxidative burst by neutrophils, decreases generation of ROS (reactive oxygen species) by neutrophils and reduces chemotaxis by neutrophils, all of which are SIgA effector functions used to stimulate the immune response. Does not block SIgA-binding to its receptor (FCAR) on neutrophils, but it decreases SIgA-stimulated phosphorylation of cytoplasmic proteins, including phospholipase C-gamma and MAP kinases, all actions that may be advantageous to the pathogen.<ref>PMID:23882011</ref>
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BACKGROUND: Increasing rates of antimicrobial resistance among uropathogens led, among other efforts, to the application of subtractive reverse vaccinology for the identification of antigens present in extraintestinal pathogenic E. coli (ExPEC) strains but absent or variable in non-pathogenic strains, in a quest for a broadly protective Escherichia coli vaccine. The protein coded by locus c5321 from CFT073 E. coli was identified as one of nine potential vaccine candidates against ExPEC and was able to confer protection with an efficacy of 33% in a mouse model of sepsis. c5321 (known also as EsiB) lacks functional annotation and structurally belongs to the Sel1-like repeat (SLR) family. Herein, as part of the general characterization of this potential antigen, we have focused on its structural properties. RESULTS: We report the 1.74 A-resolution crystal structure of c5321 from CFT073 E. coli determined by Se-Met SAD phasing. The structure is composed of 11 SLR units in a topological organisation that highly resembles that found in HcpC from Helicobacter pylori, with the main difference residing in how the super-helical fold is stabilised. The stabilising effect of disulfide bridges in HcpC is replaced in c5321 by a strengthening of the inter-repeat hydrophobic core. A metal-ion binding site, uncharacteristic of SLR proteins, is detected between SLR units 3 and 4 in the region of the inter-repeat hydrophobic core. Crystal contacts are observed between the C-terminal tail of one molecule and the C-terminal amphipathic groove of a neighbouring one, resembling interactions between ligand and proteins containing tetratricopeptide-like repeats. CONCLUSIONS: The structure of antigen c5321 presents a mode of stabilization of the SLR fold different from that observed in close homologs of known structure. The location of the metal-ion binding site and the observed crystal contacts suggest a potential role in regulation of conformational flexibility and interaction with yet unidentified target proteins, respectively. These findings open new perspectives in both antigen design and for the identification of a functional role for this protective antigen.
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Crystal structure of c5321: a protective antigen present in uropathogenic Escherichia coli strains displaying an SLR fold.,Urosev D, Ferrer-Navarro M, Pastorello I, Cartocci E, Costenaro L, Zhulenkovs D, Marechal JD, Leonchiks A, Reverter D, Serino L, Soriani M, Daura X BMC Struct Biol. 2013 Oct 7;13(1):19. PMID:24099525<ref>PMID:24099525</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4bwr" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecol6]]
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[[Category: Escherichia coli CFT073]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cartocci, E]]
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[[Category: Cartocci E]]
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[[Category: Costenaro, L]]
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[[Category: Costenaro L]]
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[[Category: Daura, X]]
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[[Category: Daura X]]
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[[Category: Ferrer-Navarro, M]]
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[[Category: Ferrer-Navarro M]]
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[[Category: Leonchiks, A]]
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[[Category: Leonchiks A]]
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[[Category: Marechal, J D]]
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[[Category: Marechal J-D]]
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[[Category: Pastorello, I]]
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[[Category: Pastorello I]]
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[[Category: Reverter, D]]
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[[Category: Reverter D]]
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[[Category: Serino, L]]
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[[Category: Serino L]]
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[[Category: Soriani, M]]
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[[Category: Soriani M]]
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[[Category: Urosev, D]]
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[[Category: Urosev D]]
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[[Category: Zhulenkovs, D]]
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[[Category: Zhulenkovs D]]
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[[Category: Sel1-like repeat]]
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[[Category: Super-helical fold]]
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[[Category: Unknown function]]
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Current revision

Crystal structure of c5321: a protective antigen present in uropathogenic Escherichia coli strains displaying an SLR fold

PDB ID 4bwr

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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