5f8r: Difference between revisions
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==Blood group antigen binding adhesin BabA of Helicobacter pylori strain S831 in complex with blood group H Lewis b hexasaccharide== | ==Blood group antigen binding adhesin BabA of Helicobacter pylori strain S831 in complex with blood group H Lewis b hexasaccharide== | ||
<StructureSection load='5f8r' size='340' side='right' caption='[[5f8r]], [[Resolution|resolution]] 2.44Å' scene=''> | <StructureSection load='5f8r' size='340' side='right'caption='[[5f8r]], [[Resolution|resolution]] 2.44Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5f8r]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F8R OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5f8r]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504] and [http://en.wikipedia.org/wiki/Camelus_glama Camelus glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F8R OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5F8R FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | </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'>[http:// | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">babA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5f8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f8r OCA], [http://pdbe.org/5f8r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f8r RCSB], [http://www.ebi.ac.uk/pdbsum/5f8r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f8r ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc 43504]] | |||
[[Category: Camelus glama]] | |||
[[Category: Large Structures]] | |||
[[Category: Boren, T]] | [[Category: Boren, T]] | ||
[[Category: Gideonsson, P]] | [[Category: Gideonsson, P]] | ||
Revision as of 11:05, 29 April 2020
Blood group antigen binding adhesin BabA of Helicobacter pylori strain S831 in complex with blood group H Lewis b hexasaccharideBlood group antigen binding adhesin BabA of Helicobacter pylori strain S831 in complex with blood group H Lewis b hexasaccharide
Structural highlights
Publication 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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