5j4f

Crystal structure of the N-terminally His6-tagged HP0902, an uncharacterized protein from Helicobacter pylori 26695

spinqualitylabelsall models 5j4f, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5j4f is a 2 chain structure with sequence from Helicobacter pylori 26695. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.4Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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