From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1ouv.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1ouv.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1ouv| PDB=1ouv | SCENE= }} | | {{STRUCTURE_1ouv| PDB=1ouv | SCENE= }} |
| | | | |
| - | '''Helicobacter cysteine rich protein C (HcpC)'''
| + | ===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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15223324}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15223324 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_15223324}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 29: |
Line 33: |
| | [[Category: Repeat protein]] | | [[Category: Repeat protein]] |
| | [[Category: Tpr repeat]] | | [[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 Mon Jul 28 14:36:02 2008'' |
Revision as of 11:36, 28 July 2008
Template:STRUCTURE 1ouv
Helicobacter cysteine rich protein C (HcpC)
Template:ABSTRACT PUBMED 15223324
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 Mon Jul 28 14:36:02 2008
