7o23

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Current revision

C-terminal head domain of the trimeric autotransporter adhesin BpaC from Burkholderia pseudomallei fused to a GCN4 anchor

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Categories: Burkholderia pseudomallei 1026b | Large Structures | Saccharomyces cerevisiae S288C | Goldman A | Kiessling AR

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 <StructureSection load='7o23' size='340' side='right'caption='[[7o23]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[7o23]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O23 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O23 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7o23]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_pseudomallei_1026b Burkholderia pseudomallei 1026b] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O23 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O23 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=7o23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o23 OCA], [https://pdbe.org/7o23 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o23 RCSB], [https://www.ebi.ac.uk/pdbsum/7o23 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o23 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/BPAC_BURP2 BPAC_BURP2]] Involved in virulence (PubMed:23716608, PubMed:24731253). Mediates adherence to human respiratory epithelial cells (PubMed:24731253).<ref>PMID:23716608</ref> <ref>PMID:24731253</ref>
+[https://www.uniprot.org/uniprot/BPAC_BURP2 BPAC_BURP2] Involved in virulence (PubMed:23716608, PubMed:24731253). Mediates adherence to human respiratory epithelial cells (PubMed:24731253).<ref>PMID:23716608</ref> <ref>PMID:24731253</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Gram-negative pathogens like Burkholderia pseudomallei use trimeric autotransporter adhesins such as BpaC as key molecules in their pathogenicity. Our 1.4 A crystal structure of the membrane-proximal part of the BpaC head domain shows that the domain is exclusively made of left-handed parallel beta-roll repeats. This, the largest such structure solved, has two unique features. First, the core, rather than being composed of the canonical hydrophobic Ile and Val, is made up primarily of the hydrophilic Thr and Asn, with two different solvent channels. Second, comparing BpaC to all other left-handed parallel beta-roll structures showed that the position of the head domain in the protein correlates with the number and type of charged residues. In BpaC, only negatively charged residues face the solvent-in stark contrast to the primarily positive surface charge of the left-handed parallel beta-roll "type" protein, YadA. We propose extending the definitions of these head domains to include the BpaC-like head domain as a separate subtype, based on its unusual sequence, position, and charge. We speculate that the function of left-handed parallel beta-roll structures may differ depending on their position in the structure.
-The C-terminal head domain of Burkholderia pseudomallei BpaC has a striking hydrophilic core with an extensive solvent network.,Kiessling AR, Harris SA, Weimer KM, Wells G, Goldman A Mol Microbiol. 2022 Jul;118(1-2):77-91. doi: 10.1111/mmi.14953. Epub 2022 Jul 1. PMID:35703459<ref>PMID:35703459</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 7o23" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Burkholderia pseudomallei 1026b]]
 [[Category: Large Structures]]
-[[Category: Goldman, A]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Kiessling, A R]]
+[[Category: Goldman A]]
-[[Category: Cell adhesion]]
+[[Category: Kiessling AR]]
-[[Category: Extracellular]]
-[[Category: Left-handed parallel beta-roll]]

7o23

From Proteopedia

Current revision

C-terminal head domain of the trimeric autotransporter adhesin BpaC from Burkholderia pseudomallei fused to a GCN4 anchor

Structural highlights

Function

References

Contents

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