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| | ==Crystal structure of SabA from Helicobacter pylori== | | ==Crystal structure of SabA from Helicobacter pylori== |
| - | <StructureSection load='4o5j' size='340' side='right' caption='[[4o5j]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='4o5j' size='340' side='right'caption='[[4o5j]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4o5j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Campylobacter_pylori Campylobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O5J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O5J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4o5j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O5J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O5J FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C694_03730, SabA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85962 Campylobacter pylori])</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=4o5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o5j OCA], [https://pdbe.org/4o5j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o5j RCSB], [https://www.ebi.ac.uk/pdbsum/4o5j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o5j ProSAT]</span></td></tr> |
| - | <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=4o5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o5j OCA], [http://pdbe.org/4o5j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o5j RCSB], [http://www.ebi.ac.uk/pdbsum/4o5j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o5j ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A2I8VBX7_HELPX A0A2I8VBX7_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: Campylobacter pylori]] | + | [[Category: Helicobacter pylori 26695]] |
| - | [[Category: Nguyen, S T.S]] | + | [[Category: Large Structures]] |
| - | [[Category: Pang, S S]] | + | [[Category: Nguyen STS]] |
| - | [[Category: Whisstock, J C]] | + | [[Category: Pang SS]] |
| - | [[Category: Adhesin]] | + | [[Category: Whisstock JC]] |
| - | [[Category: Carbohydrate/sugar binding]]
| + | |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Helicobacter pylori]]
| + | |
| - | [[Category: Outer membrane protein]]
| + | |
| - | [[Category: Tetratricopeptide repeat]]
| + | |
| Structural highlights
Function
A0A2I8VBX7_HELPX
Publication Abstract from PubMed
The gastric pathogen Helicobacter pylori is a major cause of acute chronic gastritis and the development of stomach and duodenal ulcers. Chronic infection furthermore pre-disposes to the development of gastric cancer. Crucial to H. pylori survival within the hostile environment of the digestive system are the adhesins SabA and BabA; these molecules belong to the same protein family and permit the bacteria to bind tightly to sugar moieties LewisB and sialyl-LewisX, respectively, on the surface of epithelial cells lining the stomach and duodenum. Currently, no representative SabA / BabA structure has been determined, however, hampering the development of strategies to eliminate persistent H. pylori infections that fail to respond to conventional therapy. Here, using X-ray crystallography, we show that the soluble extracellular adhesin domain of SabA shares distant similarity to the tetratricopeptide repeat (TPR) fold family. The molecule broadly resembles a golf putter in shape, with the head region featuring a large cavity surrounded by loops that vary in sequence between different H. pylori strains. The N-terminal and C-terminal helices protrude at right angles from the head domain and together form a shaft that connects to a predicted outer membrane protein (OMP)-like beta-barrel trans-membrane domain. Using surface plasmon resonance, we were able to detect binding of the SabA adhesin domain to sialyl-LewisX and LewisX but not to LewisA, LewisB or LewisY. Substitution of the highly conserved glutamine residue 159 in the predicted ligand-binding pocket abrogates the binding of the SabA adhesin domain to sialyl-LewisX and LewisX. Taken together, these data suggest that the adhesin domain of SabA is sufficient in isolation for specific ligand binding.
The three-dimensional structure of the extracellular adhesion domain of the sialic acid-binding adhesin SabA from Helicobacter pylori.,Pang SS, Nguyen ST, Perry AJ, Day CJ, Panjikar S, Tiralongo J, Whisstock JC, Kwok T J Biol Chem. 2013 Dec 27. PMID:24375407[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pang SS, Nguyen ST, Perry AJ, Day CJ, Panjikar S, Tiralongo J, Whisstock JC, Kwok T. The three-dimensional structure of the extracellular adhesion domain of the sialic acid-binding adhesin SabA from Helicobacter pylori. J Biol Chem. 2013 Dec 27. PMID:24375407 doi:http://dx.doi.org/10.1074/jbc.M113.513135
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