1S2X

Crystal structure of Cag-Z from Helicobacter pylori

Summary for 1S2X

• Entry DOI: 10.2210/pdb1s2x/pdb
• Descriptor: Cag-Z, ISOPROPYL ALCOHOL (3 entities in total)
• Functional Keywords: cag-z, helicobacter pylori, cag pathogenicity island, type iv secretion system, unknown function
• Biological source: Helicobacter pylori
• Total number of polymer chains: 1
• Total formula weight: 23998.47

Authors

Cendron, L.,Seydel, A.,Angelini, A.,Battistutta, R.,Zanotti, G. (deposition date: 2004-01-12, release date: 2004-07-27, Last modification date: 2024-11-20)

Primary citation

Cendron, L.,Seydel, A.,Angelini, A.,Battistutta, R.,Zanotti, G.
Crystal structure of CagZ, a protein from the Helicobacter pylori pathogenicity island that encodes for a type IV secretion system
J.Mol.Biol., 340:881-889, 2004

PubMed Abstract: CagZ, a 23 kDa protein encoded by the cagZ gene (HP0526) of the cag pathogenicity island of Helicobacter pylori, has been cloned, over-expressed, purified and its three-dimensional structure determined. The protein consists of a single compact L-shaped domain, composed of seven alpha-helices including about 70% of the total residues. Three-dimensional homology searches did not reveal structural homologues, and CagZ can be considered representative of a new protein fold. The presence of a disordered C-terminal tail and the nature of the molecular surface suggest that CagZ may participate in the interaction of effector proteins with one or more components of the H.pylori type IV secretion system on the cytoplasmic side of the inner membrane.

PubMed: 15223328
DOI: 10.1016/j.jmb.2004.05.016

Experimental method

X-RAY DIFFRACTION (1.9 Å)