1H79

STRUCTURAL BASIS FOR ALLOSTERIC SUBSTRATE SPECIFICITY REGULATION IN CLASS III RIBONUCLEOTIDE REDUCTASES: NRDD IN COMPLEX WITH DTTP

Summary for 1H79

• Entry DOI: 10.2210/pdb1h79/pdb
• Related: 1H77 1H78 1H7A 1H7B
• Descriptor: ANAEROBIC RIBONUCLEOTIDE-TRIPHOSPHATE REDUCTASE LARGE CHAIN, THYMIDINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: oxidoreductase, reductase, allosteric regulation, substrate specificity
• Biological source: BACTERIOPHAGE T4
• Total number of polymer chains: 1
• Total formula weight: 69100.08

Authors

Larsson, K.-M.,Andersson, J.,Sjoeberg, B.-M.,Nordlund, P.,Logan, D.T. (deposition date: 2001-07-04, release date: 2002-03-28, Last modification date: 2023-12-13)

Primary citation

Larsson, K.-M.,Andersson, J.,Sjoeberg, B.-M.,Nordlund, P.,Logan, D.T.
Structural Basis for Allosteric Substrate Specificty Regulation in Anaerobic Ribonucleotide Reductase
Structure, 9:739-, 2001

PubMed Abstract: 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.

PubMed: 11587648
DOI: 10.1016/S0969-2126(01)00627-X

Experimental method

X-RAY DIFFRACTION (2.9 Å)