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.


2hze

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2hze.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2hze.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2hze| PDB=2hze | SCENE= }}
{{STRUCTURE_2hze| PDB=2hze | SCENE= }}
-
'''Crystal structures of a poxviral glutaredoxin in the oxidized and reduced states show redox-correlated structural changes'''
+
===Crystal structures of a poxviral glutaredoxin in the oxidized and reduced states show redox-correlated structural changes===
-
==Overview==
+
<!--
-
Glutaredoxins act as reducing agents for the large subunit of ribonucleotide reductase (R1) in many prokaryotes and eukaryotes, including humans. The same relationship has been proposed for the glutaredoxin and R1 proteins expressed by all orthopoxviruses, including vaccinia, variola, and ectromelia virus. Interestingly, the orthopoxviral proteins share 45% and 78% sequence identity with human glutaredoxin-1 (Grx-1) and R1, respectively. To study structure-function relationships of the vertebrate Grx-1 family, and reveal potential viral adaptations, we have determined crystal structures of the ectromelia virus glutaredoxin, EVM053, in the oxidized and reduced states. The structures show a large redox-induced conformational rearrangement of Tyr21 and Thr22 near the active site. We predict that the movement of Tyr21 is a viral-specific adaptation that increases the redox potential by stabilizing the reduced state. The conformational switch of Thr22 appears to be shared by vertebrate Grx-1 and may affect the strictly conserved Lys20. A crystal packing-induced structural change in residues 68-70 affects the GSH-binding loop, and our structures reveal a potential interaction network that connects the GSH-binding loop and the active site. EVM053 also exhibits a novel cis-proline (Pro53) in a loop that has been shown to contribute to R1-binding in Escherichia coli Grx-1. The cis-peptide bond of Pro53 may be required to promote electrostatic interactions between Lys52 and the C-terminal carboxylate of R1. Finally, dimethylarsenite was covalently attached to Cys23 in one reduced EVM053 structure and our preliminary data show that EVM053 has dimethylarsenate reductase activity.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17137595}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17137595 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17137595}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Dimethylarsenite.]]
[[Category: Dimethylarsenite.]]
[[Category: Thioredoxin fold]]
[[Category: Thioredoxin fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:53:54 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:20:11 2008''

Revision as of 17:20, 27 July 2008

Image:2hze.png

Template:STRUCTURE 2hze

Crystal structures of a poxviral glutaredoxin in the oxidized and reduced states show redox-correlated structural changes

Template:ABSTRACT PUBMED 17137595

About this Structure

2HZE is a Protein complex structure of sequences from Ectromelia virus. Full crystallographic information is available from OCA.

Reference

Crystal structures of a poxviral glutaredoxin in the oxidized and reduced states show redox-correlated structural changes., Bacik JP, Hazes B, J Mol Biol. 2007 Feb 2;365(5):1545-58. Epub 2006 Nov 6. PMID:17137595

Page seeded by OCA on Sun Jul 27 20:20:11 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2hze"
Personal tools