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.


1jqc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1jqc.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1jqc.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1jqc| PDB=1jqc | SCENE= }}
{{STRUCTURE_1jqc| PDB=1jqc | SCENE= }}
-
'''Mn substituted Ribonucleotide reductase R2 from E. Coli oxidized by hydrogen peroxide and hydroxylamine'''
+
===Mn substituted Ribonucleotide reductase R2 from E. Coli oxidized by hydrogen peroxide and hydroxylamine===
-
==Overview==
+
<!--
-
The di-iron carboxylate proteins constitute a diverse class of non-heme iron enzymes performing a multitude of redox reactions. These reactions usually involve high-valent Fe-oxo species and are thought to be controlled by carboxylate shifts. Owing to their short lifetime, the intermediate structures have so far escaped structural characterization by X-ray crystallography. In an attempt to map the carboxylate conformations available to the protein during different redox states and different ligand environments, we have studied metal-substituted forms of the R2 protein of ribonucleotide reductase from Escherichia coli. In the present work we have solved the crystal structures of Mn-substituted R2 oxidized in two different ways. Oxidation was performed using either nitric oxide or a combination of hydrogen peroxide and hydroxylamine. The two structures are virtually identical, indicating that the oxidation states are the same, most likely a mixed-valent MnII-MnIII centre. One of the carboxylate ligands (D84) adopts a new, so far unseen, conformation, which could participate in the mechanism for radical generation in R2. E238 adopts a bridging-chelating conformation proposed to be important for proper O2 activation but not previously observed in the wild-type enzyme. Probable catalase activity was also observed during the oxidation with H2O2, indicating mechanistic similarities to the di-Mn catalases.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11315567}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11315567 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11315567}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Radical protein]]
[[Category: Radical protein]]
[[Category: Ribonucleotide reductase r2]]
[[Category: Ribonucleotide reductase r2]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:38:02 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:38:14 2008''

Revision as of 17:38, 1 July 2008

Image:1jqc.png

Template:STRUCTURE 1jqc

Mn substituted Ribonucleotide reductase R2 from E. Coli oxidized by hydrogen peroxide and hydroxylamine

Template:ABSTRACT PUBMED 11315567

About this Structure

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

Reference

Crystal structures of oxidized dinuclear manganese centres in Mn-substituted class I ribonucleotide reductase from Escherichia coli: carboxylate shifts with implications for O2 activation and radical generation., Hogbom M, Andersson ME, Nordlund P, J Biol Inorg Chem. 2001 Mar;6(3):315-23. PMID:11315567

Page seeded by OCA on Tue Jul 1 20:38:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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