6bea

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Current revision (14:21, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6bea' size='340' side='right'caption='[[6bea]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
<StructureSection load='6bea' size='340' side='right'caption='[[6bea]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6bea]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecol6 Ecol6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BEA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BEA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6bea]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_CFT073 Escherichia coli CFT073]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BEA 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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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]] 1.97&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kh3|4kh3]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">c0426 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=199310 ECOL6])</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=6bea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bea OCA], [https://pdbe.org/6bea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bea RCSB], [https://www.ebi.ac.uk/pdbsum/6bea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bea 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=6bea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bea OCA], [http://pdbe.org/6bea PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bea RCSB], [http://www.ebi.ac.uk/pdbsum/6bea PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bea 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/A0A0H2V5A3_ECOL6 A0A0H2V5A3_ECOL6]
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Autotransporters are the largest family of outer membrane and secreted proteins in Gram-negative bacteria. Most autotransporters are localised to the bacterial surface where they promote colonisation of host epithelial surfaces. Here we present the crystal structure of UpaB, an autotransporter that is known to contribute to uropathogenic E. coli (UPEC) colonisation of the urinary tract. We provide evidence that UpaB can interact with glycosaminoglycans and host fibronectin. Unique modifications to its core beta-helical structure create a groove on one side of the protein for interaction with glycosaminoglycans, while the opposite face can bind fibronectin. Our findings reveal far greater diversity in the autotransporter beta-helix than previously thought, and suggest that this domain can interact with host macromolecules. The relevance of these interactions during infection remains unclear.
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Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules.,Paxman JJ, Lo AW, Sullivan MJ, Panjikar S, Kuiper M, Whitten AE, Wang G, Luan CH, Moriel DG, Tan L, Peters KM, Phan MD, Gee CL, Ulett GC, Schembri MA, Heras B Nat Commun. 2019 Apr 29;10(1):1967. doi: 10.1038/s41467-019-09814-6. PMID:31036849<ref>PMID:31036849</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 6bea" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__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: Heras, B]]
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[[Category: Heras B]]
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[[Category: Paxman, J J]]
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[[Category: Paxman JJ]]
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[[Category: Autotransporter protein]]
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[[Category: Bacterial adhesin]]
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[[Category: Fibronectin]]
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[[Category: Glycosaminoglycan]]
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[[Category: Protein binding]]
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[[Category: Virulence factor]]
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Current revision

Crystal structure of the autotransporter UpaB from E. coli strain CFT073

PDB ID 6bea

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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