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.


1zof

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1zof.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1zof.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1zof| PDB=1zof | SCENE= }}
{{STRUCTURE_1zof| PDB=1zof | SCENE= }}
-
'''Crystal structure of alkyl hydroperoxide-reductase (AhpC) from Helicobacter Pylori'''
+
===Crystal structure of alkyl hydroperoxide-reductase (AhpC) from Helicobacter Pylori===
-
==Overview==
+
<!--
-
The AhpC protein from H. pylori, a thioredoxin (Trx)-dependent alkyl hydroperoxide-reductase, is a member of the ubiquitous 2-Cys peroxiredoxins family (2-Cys Prxs), a group of thiol-specific antioxidant enzymes. Prxs exert the protective antioxidant role in cells through their peroxidase activity, whereby hydrogen peroxide, peroxynitrite and a wide range of organic hydroperoxides (ROOH) are reduced and detoxified (ROOH + 2e(-)--&gt;ROH + H2O). In this study AhpC has been cloned and overexpressed in E. coli. After purification to homogeneity, crystals of the recombinant protein were grown. They diffract to 2.95 A resolution using synchrotron radiation. The crystal structure of AhpC has been determined using the molecular replacement method (R = 23.6%, R(free) = 25.9%). The model, similar in the overall to other members of the 2-Cys Prx family crystallized as toroide-shaped complexes, consists of a pentameric arrangement of homodimers [(alpha2)5 decamer]. The model of AhpC from H. pylori presents significant differences with respect to other members of the family: apart from some loop regions, alpha5-helix and the C-terminus is shifted, preventing the C-terminal tail of the second subunit from extending toward this region of the molecule. Oligomerization properties of AhpC have been also characterized by gel filtration chromatography.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16213196}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16213196 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16213196}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Decamer]]
[[Category: Decamer]]
[[Category: Toroide-shaped complex]]
[[Category: Toroide-shaped complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:52:35 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:31:07 2008''

Revision as of 21:31, 28 July 2008

Template:STRUCTURE 1zof

Crystal structure of alkyl hydroperoxide-reductase (AhpC) from Helicobacter Pylori

Template:ABSTRACT PUBMED 16213196

About this Structure

1ZOF is a Single protein structure of sequence from Helicobacter pylori. Full crystallographic information is available from OCA.

Reference

Crystal structure of alkyl hydroperoxide-reductase (AhpC) from Helicobacter pylori., Papinutto E, Windle HJ, Cendron L, Battistutta R, Kelleher D, Zanotti G, Biochim Biophys Acta. 2005 Dec 1;1753(2):240-6. Epub 2005 Sep 21. PMID:16213196

Page seeded by OCA on Tue Jul 29 00:31:07 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools