1M15

Transition state structure of arginine kinase

1M15 の概要

• エントリーDOI: 10.2210/pdb1m15/pdb
• 分子名称: arginine kinase, NITRATE ION, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: arginine kinase, creatine kinase, phosphagen kinase, transition state analog, adenosine triphosphate, transferase
• 由来する生物種: Limulus polyphemus (Atlantic horseshoe crab)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41000.48

構造登録者

Yousef, M.S.,Fabiola, F.,Gattis, J.L.,Somasundaram, T.,Chapman, M.S. (登録日: 2002-06-17, 公開日: 2002-12-04, 最終更新日: 2024-02-14)

主引用文献

Yousef, M.S.,Fabiola, F.,Gattis, J.L.,Somasundaram, T.,Chapman, M.S.
Refinement of the arginine kinase transition-state analogue complex at 1.2 A resolution: mechanistic insights.
Acta Crystallogr.,Sect.D, 58:2009-2017, 2002

PubMed Abstract: The three-dimensional crystal structure of an arginine kinase transition-state analogue complex has been refined at 1.2 A resolution, with an overall R factor of 12.3%. The current model provides a unique opportunity to analyze the structure of a bimolecular (phosphagen kinase) enzyme in its transition state. This atomic resolution structure confirms in-line transfer of the phosphoryl group and the catalytic importance of the precise alignment of the substrates. The structure is consistent with a concerted proton transfer that has been proposed for an unrelated kinase. Refinement of anisotropic temperature factors and translation-libration-screw (TLS) analyses led to the identification of four rigid groups and their prevalent modes of motion in the transition state. The relative magnitudes of the mobility of rigid groups are consistent with their proposed roles in catalysis.

PubMed: 12454458
DOI: 10.1107/S0907444902014683

実験手法

X-RAY DIFFRACTION (1.2 Å)