5J4G

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

Summary for 5J4G

• Entry DOI: 10.2210/pdb5j4g/pdb
• Related: 5J4F
• Descriptor: Uncharacterized protein (2 entities in total)
• Functional Keywords: hp0902, helicobacter pylori, secretory protein, cupin family, uncharacterized protein, unknown function
• Biological source: Helicobacter pylori (strain ATCC 700392 / 26695)
• Total number of polymer chains: 2
• Total formula weight: 24238.33

Authors

Sim, D.W.,Lee, W.C.,Kim, H.Y.,Kim, J.H.,Won, H.S. (deposition date: 2016-04-01, release date: 2017-02-08, Last modification date: 2023-11-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.6 Å)