4GW2

Crystal structure of arginine kinase in complex with L-ornithine, MgADP, and nitrate.

4GW2 の概要

• エントリーDOI: 10.2210/pdb4gw2/pdb
• 関連するPDBエントリー: 1M15 3M10 4GVY 4GVZ 4GW0
• 分子名称: Arginine kinase, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: arginine kinase, phosphagen kinase, transferase, transition state analog, kinase
• 由来する生物種: Limulus polyphemus (Atlantic horseshoe crab)
• 細胞内の位置: Cytoplasm: P51541
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40895.43

構造登録者

Clark, S.A.,Davulcu, O.,Chapman, M.S. (登録日: 2012-08-31, 公開日: 2012-10-03, 最終更新日: 2023-09-13)

主引用文献

Clark, S.A.,Davulcu, O.,Chapman, M.S.
Crystal structures of arginine kinase in complex with ADP, nitrate, and various phosphagen analogs.
Biochem.Biophys.Res.Commun., 427:212-217, 2012

PubMed Abstract: Arginine kinase catalyzes the reversible transfer of a phosphoryl group between ATP and l-arginine and is a monomeric homolog of the human enzyme creatine kinase. Arginine and creatine kinases belongs to the phosphagen kinase family of enzymes, which consists of eight known members, each of which is specific for its own phosphagen. Here, the source of phosphagen specificity in arginine kinase is investigated through the use of phosphagen analogs. Crystal structures have been determined for Limulus polyphemus arginine kinase with one of four arginine analogs bound in a transition state analog complex: l-ornithine, l-citrulline, imino-l-ornithine, and d-arginine. In all complexes, the enzyme achieves a closed conformation very similar to that of the cognate transition state analog complex, but differences are observed in the configurations of bound ligands. Arginine kinase exhibits no detectable activity towards ornithine, citrulline, or imino-l-ornithine, and only trace activity towards d-arginine. The crystal structures presented here demonstrate that phosphagen specificity is derived neither from a lock-and-key mechanism nor a modulation of induced-fit conformational changes, but potentially from subtle distortions in bound substrate configurations.

PubMed: 22995310
DOI: 10.1016/j.bbrc.2012.09.053

実験手法

X-RAY DIFFRACTION (2.157 Å)