5f7m: Difference between revisions
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The | ==Blood group antigen binding adhesin BabA of Helicobacter pylori strain 17875 in complex with blood group H Lewis b hexasaccharide== | ||
<StructureSection load='5f7m' size='340' side='right'caption='[[5f7m]], [[Resolution|resolution]] 2.72Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5f7m]] 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=5F7M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F7M FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.72Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=5f7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f7m OCA], [https://pdbe.org/5f7m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f7m RCSB], [https://www.ebi.ac.uk/pdbsum/5f7m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f7m ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/O52269_HELPX O52269_HELPX] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The 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<ref>PMID:26764597</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5f7m" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Gideonsson | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Helicobacter pylori]] | ||
[[Category: | [[Category: Lama glama]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Boren T]] | |||
[[Category: Gideonsson P]] | |||
[[Category: Moonens K]] | |||
[[Category: Muyldermans S]] | |||
[[Category: Oscarson S]] | |||
[[Category: Remaut H]] | |||
[[Category: Romao E]] | |||
[[Category: Subedi S]] | |||
Latest revision as of 09:41, 19 July 2023
Blood group antigen binding adhesin BabA of Helicobacter pylori strain 17875 in complex with blood group H Lewis b hexasaccharideBlood group antigen binding adhesin BabA of Helicobacter pylori strain 17875 in complex with blood group H Lewis b hexasaccharide
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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