1h7b
From Proteopedia
| Line 26: | Line 26: | ||
[[Category: substrate specificity]] | [[Category: substrate specificity]] | ||
| - | ''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 15:31:11 2007'' |
Revision as of 13:26, 30 October 2007
|
STRUCTURAL BASIS FOR ALLOSTERIC SUBSTRATE SPECIFICITY REGULATION IN CLASS III RIBONUCLEOTIDE REDUCTASES, NATIVE NRDD
Overview
BACKGROUND: The specificity of ribonucleotide reductases (RNRs) toward, their four substrates is governed by the binding of deoxyribonucleoside, triphosphates (dNTPs) to the allosteric specificity site. Similar patterns, in the kinetics of allosteric regulation have been a strong argument for a, common evolutionary origin of the three otherwise widely divergent RNR, classes. Recent structural information settled the case for divergent, evolution; however, the structural basis for transmission of the, allosteric signal is currently poorly understood. A comparative study of, the conformational effects of the binding of different effectors has not, yet been possible; in addition, only one RNR class has been studied., RESULTS: Our presentation of the structures of a class III anaerobic RNR, ... [(full description)]
About this Structure
1H7B is a [Single protein] structure of sequence from [Enterobacteria phage t2] with PO4 as [ligand]. Active as [Ribonucleoside-triphosphate reductase], with EC number [1.17.4.2]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Structural basis for allosteric substrate specificity regulation in anaerobic ribonucleotide reductases., Larsson KM, Andersson J, Sjoberg BM, Nordlund P, Logan DT, Structure. 2001 Aug;9(8):739-50. PMID:11587648
Page seeded by OCA on Tue Oct 30 15:31:11 2007
