This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1ouv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
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

Image:1ouv.png

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ouv"
Personal tools