1OUV

Helicobacter cysteine rich protein C (HcpC)

Summary for 1OUV

• Entry DOI: 10.2210/pdb1ouv/pdb
• Related: 1klx
• Descriptor: conserved hypothetical secreted protein (2 entities in total)
• Functional Keywords: tpr repeat, hcp repeat, cysteine rich protein, loop-helix-turn-helix, repeat protein, hydrolase
• Biological source: Helicobacter pylori
• Cellular location: Secreted (Potential): O25728
• Total number of polymer chains: 1
• Total formula weight: 29971.95

Authors

Mittl, P.R.,Luethy, L. (deposition date: 2003-03-25, release date: 2004-03-30, Last modification date: 2024-10-30)

Primary citation

Luethy, L.,Grutter, M.G.,Mittl, P.R.
The Crystal Structure of Helicobacter Cysteine-rich Protein C at 2.0A Resolution: Similar Peptide-binding Sites in TPR and SEL1-like Repeat Proteins
J.Mol.Biol., 340:829-841, 2004

PubMed Abstract: 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.

PubMed: 15223324
DOI: 10.1016/j.jmb.2004.04.055

Experimental method

X-RAY DIFFRACTION (2 Å)