1H79

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

1H79 の概要

• エントリーDOI: 10.2210/pdb1h79/pdb
• 関連するPDBエントリー: 1H77 1H78 1H7A 1H7B
• 分子名称: ANAEROBIC RIBONUCLEOTIDE-TRIPHOSPHATE REDUCTASE LARGE CHAIN, THYMIDINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, reductase, allosteric regulation, substrate specificity
• 由来する生物種: BACTERIOPHAGE T4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 69100.08

構造登録者

Larsson, K.-M.,Andersson, J.,Sjoeberg, B.-M.,Nordlund, P.,Logan, D.T. (登録日: 2001-07-04, 公開日: 2002-03-28, 最終更新日: 2023-12-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.9 Å)