5f8q: Difference between revisions
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<StructureSection load='5f8q' size='340' side='right'caption='[[5f8q]], [[Resolution|resolution]] 2.59Å' scene=''> | <StructureSection load='5f8q' size='340' side='right'caption='[[5f8q]], [[Resolution|resolution]] 2.59Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5f8q]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5f8q]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori] and [https://en.wikipedia.org/wiki/Lama_glama Lama glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F8Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F8Q FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.59Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5f8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f8q OCA], [https://pdbe.org/5f8q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f8q RCSB], [https://www.ebi.ac.uk/pdbsum/5f8q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f8q ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6DSZ5_HELPX Q6DSZ5_HELPX] [https://www.uniprot.org/uniprot/O52269_HELPX O52269_HELPX] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Helicobacter pylori]] | ||
[[Category: | [[Category: Lama glama]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Boren | [[Category: Boren T]] | ||
[[Category: Gideonsson | [[Category: Gideonsson P]] | ||
[[Category: Moonens | [[Category: Moonens K]] | ||
[[Category: Muyldermans | [[Category: Muyldermans S]] | ||
[[Category: Oscarson | [[Category: Oscarson S]] | ||
[[Category: Remaut | [[Category: Remaut H]] | ||
[[Category: Romao | [[Category: Romao E]] | ||
[[Category: Subedi | [[Category: Subedi S]] | ||
Latest revision as of 09:42, 19 July 2023
Blood group antigen binding adhesin BabA of Helicobacter pylori strain S831 in complex with Nanobody Nb-ER19Blood group antigen binding adhesin BabA of Helicobacter pylori strain S831 in complex with Nanobody Nb-ER19
Structural highlights
FunctionPublication Abstract from PubMedThe Helicobacter pylori adhesin BabA binds mucosal ABO/Le(b) blood group (bg) carbohydrates. BabA facilitates bacterial attachment to gastric surfaces, increasing strain virulence and forming a recognized risk factor for peptic ulcers and gastric cancer. High sequence variation causes BabA functional diversity, but the underlying structural-molecular determinants are unknown. We generated X-ray structures of representative BabA isoforms that reveal a polymorphic, three-pronged Le(b) binding site. Two diversity loops, DL1 and DL2, provide adaptive control to binding affinity, notably ABO versus O bg preference. H. pylori strains can switch bg preference with single DL1 amino acid substitutions, and can coexpress functionally divergent BabA isoforms. The anchor point for receptor binding is the embrace of an ABO fucose residue by a disulfide-clasped loop, which is inactivated by reduction. Treatment with the redox-active pharmaceutic N-acetylcysteine lowers gastric mucosal neutrophil infiltration in H. pylori-infected Le(b)-expressing mice, providing perspectives on possible H. pylori eradication therapies. Structural Insights into Polymorphic ABO Glycan Binding by Helicobacter pylori.,Moonens K, Gideonsson P, Subedi S, Bugaytsova J, Romao E, Mendez M, Norden J, Fallah M, Rakhimova L, Shevtsova A, Lahmann M, Castaldo G, Brannstrom K, Coppens F, Lo AW, Ny T, Solnick JV, Vandenbussche G, Oscarson S, Hammarstrom L, Arnqvist A, Berg DE, Muyldermans S, Boren T, Remaut H Cell Host Microbe. 2016 Jan 13;19(1):55-66. doi: 10.1016/j.chom.2015.12.004. PMID:26764597[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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