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1ouv
From Proteopedia
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[[Image:1ouv.gif|left|200px]] | [[Image:1ouv.gif|left|200px]] | ||
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'''Helicobacter cysteine rich protein C (HcpC)''' | '''Helicobacter cysteine rich protein C (HcpC)''' | ||
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[[Category: Luethy, L.]] | [[Category: Luethy, L.]] | ||
[[Category: Mittl, P R.]] | [[Category: Mittl, P R.]] | ||
| - | [[Category: | + | [[Category: Cysteine rich protein]] |
| - | [[Category: | + | [[Category: Hcp repeat]] |
| - | [[Category: | + | [[Category: Loop-helix-turn-helix]] |
| - | [[Category: | + | [[Category: Repeat protein]] |
| - | [[Category: | + | [[Category: Tpr repeat]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:18:29 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 01:18, 3 May 2008
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 Page seeded by OCA on Sat May 3 04:18:29 2008
