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.


1hyu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hyu.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1hyu.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hyu| PDB=1hyu | SCENE= }}
{{STRUCTURE_1hyu| PDB=1hyu | SCENE= }}
-
'''CRYSTAL STRUCTURE OF INTACT AHPF'''
+
===CRYSTAL STRUCTURE OF INTACT AHPF===
-
==Overview==
+
<!--
-
AhpF, a homodimer of 57 kDa subunits, is a flavoenzyme which catalyzes the NADH-dependent reduction of redox-active disulfide bonds in the peroxidase AhpC, a member of the recently identified peroxiredoxin class of antioxidant enzymes. The structure of AhpF from Salmonella typhimurium at 2.0 A resolution, determined using multiwavelength anomalous dispersion, shows that the C-terminal portion of AhpF (residues 210-521) is structurally like Escherichia coli thioredoxin reductase. In addition, AhpF has an N-terminal domain (residues 1-196) formed from two contiguous thioredoxin folds, but containing just a single redox-active disulfide (Cys129-Cys132). A flexible linker (residues 197-209) connects the domains, consistent with experiments showing that the N-terminal domain acts as an appended substrate, first being reduced by the C-terminal portion of AhpF, and subsequently reducing AhpC. Modeling studies imply that an intrasubunit electron transfer accounts for the reduction of the N-terminal domain in dimeric AhpF. Furthermore, comparing the N-terminal domain with protein disulfide oxidoreductase from Pyrococcus furiosis, we describe a new class of protein disulfide oxidoreductases based on a novel mirror-image active site arrangement, with a distinct carboxylate (Glu86) being functionally equivalent to the key acid (Asp26) of E. coli thioredoxin. A final fortuitous result is that the N-terminal redox center is reduced and provides a high-resolution view of the thiol-thiolate hydrogen bond that has been predicted to stabilize the attacking thiolate in thioredoxin-like proteins.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11300769}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11300769 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11300769}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Thioredoxin]]
[[Category: Thioredoxin]]
[[Category: Thioredoxin reductase]]
[[Category: Thioredoxin reductase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:22:30 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:08:51 2008''

Revision as of 07:08, 1 July 2008

Image:1hyu.png

Template:STRUCTURE 1hyu

CRYSTAL STRUCTURE OF INTACT AHPF

Template:ABSTRACT PUBMED 11300769

About this Structure

1HYU is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.

Reference

Structure of intact AhpF reveals a mirrored thioredoxin-like active site and implies large domain rotations during catalysis., Wood ZA, Poole LB, Karplus PA, Biochemistry. 2001 Apr 3;40(13):3900-11. PMID:11300769

Page seeded by OCA on Tue Jul 1 10:08:51 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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