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| | <StructureSection load='5j4g' size='340' side='right'caption='[[5j4g]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='5j4g' size='340' side='right'caption='[[5j4g]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5j4g]] is a 2 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=5J4G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J4G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5j4g]] is a 2 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=5J4G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J4G FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5j4f|5j4f]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HP_0902 ([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=5j4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j4g OCA], [https://pdbe.org/5j4g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j4g RCSB], [https://www.ebi.ac.uk/pdbsum/5j4g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j4g 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=5j4g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j4g OCA], [http://pdbe.org/5j4g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j4g RCSB], [http://www.ebi.ac.uk/pdbsum/5j4g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j4g ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O25562_HELPY O25562_HELPY] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Campylobacter pylori]] | + | [[Category: Helicobacter pylori 26695]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kim, H Y]] | + | [[Category: Kim HY]] |
| - | [[Category: Kim, J H]] | + | [[Category: Kim JH]] |
| - | [[Category: Lee, W C]] | + | [[Category: Lee WC]] |
| - | [[Category: Sim, D W]] | + | [[Category: Sim DW]] |
| - | [[Category: Won, H S]] | + | [[Category: Won HS]] |
| - | [[Category: Cupin family]]
| + | |
| - | [[Category: Helicobacter pylori]]
| + | |
| - | [[Category: Hp0902]]
| + | |
| - | [[Category: Secretory protein]]
| + | |
| - | [[Category: Uncharacterized protein]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
O25562_HELPY
Publication Abstract from PubMed
We solved the crystal structure of a functionally uncharacterized protein, HP0902, from Helicobacter pylori. Its structure demonstrated an all-beta cupin fold that cannot bind metal ions due to the absence of a metal-binding histidine that is conserved in many metallo-cupins. In contrast, isothermal titration calorimetry and NMR titration demonstrated that HP0902 is able to bind bacterial endotoxin lipopolysaccharides (LPS) through its surface-exposed loops, where metal-binding sites are usually found in other metallo-cupins. This report constitutes the first identification of an LPS-interacting protein, both in the cupin family and in H. pylori. Furthermore, identification of the ability of HP0902 to bind LPS uncovers a putative role for this protein in H. pylori pathogenicity.
Structural identification of the lipopolysaccharide-binding capability of a cupin-family protein from Helicobacter pylori.,Sim DW, Kim JH, Kim HY, Jang JH, Lee WC, Kim EH, Park PJ, Lee KH, Won HS FEBS Lett. 2016 Sep;590(17):2997-3004. doi: 10.1002/1873-3468.12332. Epub 2016, Aug 11. PMID:27466800[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sim DW, Kim JH, Kim HY, Jang JH, Lee WC, Kim EH, Park PJ, Lee KH, Won HS. Structural identification of the lipopolysaccharide-binding capability of a cupin-family protein from Helicobacter pylori. FEBS Lett. 2016 Sep;590(17):2997-3004. doi: 10.1002/1873-3468.12332. Epub 2016, Aug 11. PMID:27466800 doi:http://dx.doi.org/10.1002/1873-3468.12332
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