5J4F

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

5J4F の概要

• エントリーDOI: 10.2210/pdb5j4f/pdb
• 分子名称: Uncharacterized protein (2 entities in total)
• 機能のキーワード: hp0902, helicobacter pylori, secretory protein, cupin family, uncharacterized protein, unknown function
• 由来する生物種: Helicobacter pylori (strain ATCC 700392 / 26695)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26438.76

構造登録者

Sim, D.-W.,Lee, W.-C.,Kim, H.Y.,Kim, J.-H.,Won, H.-S. (登録日: 2016-04-01, 公開日: 2017-02-08, 最終更新日: 2023-11-08)

主引用文献

Sim, D.W.,Kim, J.H.,Kim, H.Y.,Jang, J.H.,Lee, W.C.,Kim, E.H.,Park, P.J.,Lee, K.H.,Won, H.S.
Structural identification of the lipopolysaccharide-binding capability of a cupin-family protein from Helicobacter pylori
FEBS Lett., 590:2997-3004, 2016

PubMed Abstract: We solved the crystal structure of a functionally uncharacterized protein, HP0902, from Helicobacter pylori. Its structure demonstrated an all-β 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.

PubMed: 27466800
DOI: 10.1002/1873-3468.12332

実験手法

X-RAY DIFFRACTION (1.4 Å)