1pfr
From Proteopedia
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1PFR is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with FE and HG as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ | + | 1PFR is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with FE and HG as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Ribonucleoside-diphosphate_reductase Ribonucleoside-diphosphate reductase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.4.1 1.17.4.1]]. Structure known Active Sites: FE1 and FE2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PFR OCA]]. |
==Reference== | ==Reference== | ||
Crystal structure of reduced protein R2 of ribonucleotide reductase: the structural basis for oxygen activation at a dinuclear iron site., Logan DT, Su XD, Aberg A, Regnstrom K, Hajdu J, Eklund H, Nordlund P, Structure. 1996 Sep 15;4(9):1053-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8805591 8805591] | Crystal structure of reduced protein R2 of ribonucleotide reductase: the structural basis for oxygen activation at a dinuclear iron site., Logan DT, Su XD, Aberg A, Regnstrom K, Hajdu J, Eklund H, Nordlund P, Structure. 1996 Sep 15;4(9):1053-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8805591 8805591] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| + | [[Category: Ribonucleoside-diphosphate reductase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Aberg, A.]] | [[Category: Aberg, A.]] | ||
| Line 29: | Line 30: | ||
[[Category: reductase]] | [[Category: reductase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:16:07 2007'' |
Revision as of 08:11, 30 October 2007
|
RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 1 BETA CHAIN
Overview
BACKGROUND. Ribonucleotide reductases (RNRs) catalyze the formation of the, deoxyribonucleotides that are essential for DNA synthesis. The R2 subunit, of Escherichia coli RNR is a homodimer containing one dinuclear iron, centre per monomer. A tyrosyl radical is essential for catalysis, and is, formed via a reaction in which the reduced, diferrous form of the iron, centre activates dioxygen. To help understand the mechanism of oxygen, activation, we examined the structure of the diferrous form of R2., RESULTS. The crystal structures of reduced forms of both wild type R2 and, a mutant of R2 (Ser211--> Ala) have been determined at 1.7 A and 2.2 A, resolution, respectively. The diferrous iron centre was compared to the, previously determined structure of the oxidized, diferric form of R2. ... [(full description)]
About this Structure
1PFR is a [Single protein] structure of sequence from [Escherichia coli] with FE and HG as [ligands]. Active as [Ribonucleoside-diphosphate reductase], with EC number [1.17.4.1]. Structure known Active Sites: FE1 and FE2. Full crystallographic information is available from [OCA].
Reference
Crystal structure of reduced protein R2 of ribonucleotide reductase: the structural basis for oxygen activation at a dinuclear iron site., Logan DT, Su XD, Aberg A, Regnstrom K, Hajdu J, Eklund H, Nordlund P, Structure. 1996 Sep 15;4(9):1053-64. PMID:8805591
Page seeded by OCA on Tue Oct 30 10:16:07 2007
