1KLX

Helicobacter pylori cysteine rich protein B (hcpB)

Summary for 1KLX

• Entry DOI: 10.2210/pdb1klx/pdb
• Descriptor: Cysteine Rich Protein B (2 entities in total)
• Functional Keywords: structural genomics, helix-turn-helix, right handed super helix, modular structure', hydrolase
• Biological source: Helicobacter pylori
• Total number of polymer chains: 1
• Total formula weight: 15367.74

Authors

Luethy, L.,Gruetter, M.G.,Mittl, P.R.E. (deposition date: 2001-12-13, release date: 2002-09-11, Last modification date: 2024-11-06)

Primary citation

Luthy, L.,Grutter, M.G.,Mittl, P.R.
The crystal structure of Helicobacter pylori cysteine-rich protein B reveals a novel fold for a penicillin-binding protein.
J.Biol.Chem., 277:10187-10193, 2002

PubMed Abstract: Colonization of the gastric mucosa with the spiral-shaped Gram-negative proteobacterium Helicobacter pylori is probably the most common chronic infection in humans. The genomes of H. pylori strains J99 and 26695 have been completely sequenced. Functional and three-dimensional structural information is available for less than one third of all open reading frames. We investigated the function and three-dimensional structure of a member from a family of cysteine-rich hypothetical proteins that are unique to H. pylori and Campylobacter jejuni. The structure of H. pylori cysteine-rich protein (Hcp) B possesses a modular architecture consisting of four alpha/alpha-motifs that are cross-linked by disulfide bridges. The Hcp repeat is similar to the tetratricopeptide repeat, which is frequently found in protein/protein interactions. In contrast to the tetratricopeptide repeat, the Hcp repeat is 36 amino acids long. HcpB is capable of binding and hydrolyzing 6-amino penicillinic acid and 7-amino cephalosporanic acid derivatives. The HcpB fold is distinct from the fold of any known penicillin-binding protein, indicating that the Hcp proteins comprise a new family of penicillin-binding proteins. The putative penicillin binding site is located in an amphipathic groove on the concave side of the molecule.

PubMed: 11777911
DOI: 10.1074/jbc.M108993200

Experimental method

X-RAY DIFFRACTION (1.95 Å)