Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2PT7

Crystal structure of Cag VirB11 (HP0525) and an inhibitory protein (HP1451)

Summary for 2PT7
Entry DOI10.2210/pdb2pt7/pdb
Related1G6O 1NLY 1NLZ 1OPX 2GZA
DescriptorCag-alfa, Hypothetical protein (3 entities in total)
Functional Keywordsatpase, protein-protein complex, type iv secretion, hydrolase-protein binding complex, hydrolase/protein binding
Biological sourceHelicobacter pylori
More
Total number of polymer chains8
Total formula weight260953.73
Authors
Hare, S.,Fischer, W.,Williams, R.,Terradot, L.,Bayliss, R.,Haas, R.,Waksman, G. (deposition date: 2007-05-08, release date: 2007-11-13, Last modification date: 2023-08-30)
Primary citationHare, S.,Fischer, W.,Williams, R.,Terradot, L.,Bayliss, R.,Haas, R.,Waksman, G.
Identification, structure and mode of action of a new regulator of the Helicobacter pylori HP0525 ATPase.
Embo J., 26:4926-4934, 2007
Cited by
PubMed Abstract: Helicobacter pylori is one of the world's most successful human pathogens causing gastric ulcers and cancers. A key virulence factor of H. pylori is the Cag pathogenicity island, which encodes a type IV secretion system. HP0525 is an essential component of the Cag system and acts as an inner membrane associated ATPase. HP0525 forms double hexameric ring structures, with the C-terminal domains (CTDs) forming a closed ring and the N-terminal domains (NTDs) forming a dynamic, open ring. Here, the crystal structure of HP0525 in complex with a fragment of HP1451, a protein of previously unknown function, is reported. The HP1451 construct consists of two domains similar to nucleic acid-binding domains. Two HP1451 molecules bind to the HP0525 NTDs on opposite sides of the hexamer, locking it in the closed form and forming a partial lid over the HP0525 chamber. From the structure, it is suggested that HP1451 acts as an inhibitory factor of HP0525 to regulate Cag-mediated secretion, a suggestion confirmed by results of in vitro ATPase assay and in vivo pull-down experiments.
PubMed: 17972918
DOI: 10.1038/sj.emboj.7601904
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

237735

数据于2025-06-18公开中

PDB statisticsPDBj update infoContact PDBjnumon