1ouv
From Proteopedia
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Helicobacter cysteine rich protein C (HcpC)
Overview
Helicobacter pylori is a Gram-negative human pathogen that infects the, gastric mucosa and causes an inflammatory process leading to gastritis, ulceration and cancer. Bacterial cell-surface and secreted proteins often, play an important role in pathogen-host interactions and are thought to be, selective mediators for the pathology of the infection. The Helicobacter, cysteine-rich proteins (Hcp) represent a large family of secreted proteins, that seem to be specific for microorganisms from the epsilon-subfamily of, proteobacteria. Although significantly elevated levels of anti-Hcp, antibodies were observed in many patients infected with H.pylori, details, on the biological functions of Hcp proteins are sparse. Hcps belong to a, large family of Sel1-like multi-repeat proteins. The crystal structure of, HcpC was refined at 2.0 A resolution and revealed a super-helical topology, composed of seven disulfide bridged alpha/alpha-repeats, an N-terminal, capping helix and an extended C-terminal coil consisting of alternating, hydrophobic and hydrophilic residues. In the crystal packing, the, C-terminal coil interacts with the concave surface of a symmetry-related, HcpC super-helix. A hydrophobic pocket and a cluster of negatively charged, residues recognize the side-chains of Val290 and Lys287 from the, C-terminal coil, respectively. The peptide nitrogen atom of His291 forms a, short hydrogen bond with the side-chain of Asn66. The interactions seen in, this crystal contact are strikingly similar to the peptide-binding modes, of the Hsp70/Hsp90 organizing protein and the PEX5 receptor. The, conservation of the peptide-binding mode suggests that HcpC might, recognize its binding partner in a similar way.
About this Structure
1OUV is a Single protein structure of sequence from Helicobacter pylori. Full crystallographic information is available from OCA.
Reference
The crystal structure of Helicobacter cysteine-rich protein C at 2.0 A resolution: similar peptide-binding sites in TPR and SEL1-like repeat proteins., Luthy L, Grutter MG, Mittl PR, J Mol Biol. 2004 Jul 16;340(4):829-41. PMID:15223324
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