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.


1av8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1av8.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1av8.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1av8| PDB=1av8 | SCENE= }}
{{STRUCTURE_1av8| PDB=1av8 | SCENE= }}
-
'''RIBONUCLEOTIDE REDUCTASE R2 SUBUNIT FROM E. COLI'''
+
===RIBONUCLEOTIDE REDUCTASE R2 SUBUNIT FROM E. COLI===
-
==Overview==
+
<!--
-
Ribonucleotide reductase (RNR) from Escherichia coli catalyzes the conversion of ribonucleotides to deoxyribonucleotides. It is composed of two homodimeric subunits, R1 and R2. R2 contains the diferric-tyrosyl radical cofactor essential for the nucleotide reduction process. The in vitro mechanism of assembly of this cluster starting with apo R2 or with a diferrous form of R2 has been examined by time-resolved physical biochemical methods. An intermediate, Fe3+/Fe4+ cluster (intermediate X), has been identified that is thought to be directly involved in the oxidation of Y122 to the tyrosyl radical (*Y122). An R2 mutant in which phenylalanine has replaced Y122 has been used to accumulate intermediate X at sufficient levels that it can be studied using a variety of spectroscopic methods. The details of the reconstitution of the apo and diferrous forms of Y122F R2 have been examined by stopped-flow UV/vis spectroscopy and by rapid freeze quench electron paramagnetic resonance, and Mossbauer spectroscopies. In addition the structure of this mutant, crystallized at pH 7.6 in the absence of mercury, at 2.46 A resolution has been determined. These studies suggest that Y122F R2 is an appropriate model for the examination of intermediate X in the assembly process. Studies with two mutants, Y356F and double mutant Y356F and Y122F R2, are interpreted in terms of the possible role of Y356 in the putative electron transfer reaction between the R1 and R2 subunits of this RNR.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9558317}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9558317 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9558317}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Dna replication]]
[[Category: Dna replication]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:44:00 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:39:39 2008''

Revision as of 14:39, 30 June 2008

Image:1av8.png

Template:STRUCTURE 1av8

RIBONUCLEOTIDE REDUCTASE R2 SUBUNIT FROM E. COLI

Template:ABSTRACT PUBMED 9558317

About this Structure

1AV8 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Characterization of Y122F R2 of Escherichia coli ribonucleotide reductase by time-resolved physical biochemical methods and X-ray crystallography., Tong W, Burdi D, Riggs-Gelasco P, Chen S, Edmondson D, Huynh BH, Stubbe J, Han S, Arvai A, Tainer J, Biochemistry. 1998 Apr 28;37(17):5840-8. PMID:9558317

Page seeded by OCA on Mon Jun 30 17:39:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1av8"
Personal tools