1klx
From Proteopedia
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Helicobacter pylori cysteine rich protein B (hcpB)
Overview
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.
About this Structure
1KLX is a Single protein structure of sequence from Helicobacter pylori. Full crystallographic information is available from OCA.
Reference
The crystal structure of Helicobacter pylori cysteine-rich protein B reveals a novel fold for a penicillin-binding protein., Luthy L, Grutter MG, Mittl PR, J Biol Chem. 2002 Mar 22;277(12):10187-93. Epub 2002 Jan 2. PMID:11777911
Page seeded by OCA on Tue Nov 20 19:20:58 2007
