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.


1fov

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1fov.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1fov.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1fov| PDB=1fov | SCENE= }}
{{STRUCTURE_1fov| PDB=1fov | SCENE= }}
-
'''GLUTAREDOXIN 3 FROM ESCHERICHIA COLI IN THE FULLY OXIDIZED FORM'''
+
===GLUTAREDOXIN 3 FROM ESCHERICHIA COLI IN THE FULLY OXIDIZED FORM===
-
==Overview==
+
<!--
-
A high precision NMR structure of oxidized glutaredoxin 3 [C65Y] from Escherichia coli has been determined. The conformation of the active site including the disulphide bridge is highly similar to those in glutaredoxins from pig liver and T4 phage. A comparison with the previously determined structure of glutaredoxin 3 [C14S, C65Y] in a complex with glutathione reveals conformational changes between the free and substrate-bound form which includes the sidechain of the conserved, active site tyrosine residue. In the oxidized form this tyrosine is solvent exposed, while it adopts a less exposed conformation, stabilized by hydrogen bonds, in the mixed disulfide with glutathione. The structures further suggest that the formation of a covalent linkage between glutathione and glutaredoxin 3 is necessary in order to induce these structural changes upon binding of the glutathione peptide. This could explain the observed low affinity of glutaredoxins for S-blocked glutathione analogues, in spite of the fact that glutaredoxins are highly specific reductants of glutathione mixed disulfides.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11031118}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11031118 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11031118}}
==About this Structure==
==About this Structure==
-
1FOV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOV OCA].
+
1FOV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOV OCA].
==Reference==
==Reference==
Line 30: Line 34:
[[Category: Active site disulfide]]
[[Category: Active site disulfide]]
[[Category: Cis pro 53]]
[[Category: Cis pro 53]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:35:18 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:42:21 2008''

Revision as of 00:42, 1 July 2008

Template:STRUCTURE 1fov

GLUTAREDOXIN 3 FROM ESCHERICHIA COLI IN THE FULLY OXIDIZED FORM

Template:ABSTRACT PUBMED 11031118

About this Structure

1FOV is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

Reference

NMR structure of oxidized glutaredoxin 3 from Escherichia coli., Nordstrand K, Sandstrom A, Aslund F, Holmgren A, Otting G, Berndt KD, J Mol Biol. 2000 Oct 27;303(3):423-32. PMID:11031118

Page seeded by OCA on Tue Jul 1 03:42:21 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools