2IYW

Shikimate kinase from Mycobacterium tuberculosis in complex with MgATP, open LID (conf. B)

2IYW の概要

• エントリーDOI: 10.2210/pdb2iyw/pdb
• 関連するPDBエントリー: 1L4U 1L4Y 1U8A 1ZYU 2G1J 2G1K 2IYQ 2IYR 2IYS 2IYT 2IYU 2IYV 2IYX 2IYY 2IYZ
• 分子名称: SHIKIMATE KINASE, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: transferase, aromatic amino acid biosynthesis, p-loop kinase, metal- binding, shikimate kinase, shikimate pathway, nucleotide- binding, amino-acid biosynthesis, kinase, magnesium, atp-binding
• 由来する生物種: MYCOBACTERIUM TUBERCULOSIS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20214.99

構造登録者

Hartmann, M.D.,Bourenkov, G.P.,Oberschall, A.,Strizhov, N.,Bartunik, H.D. (登録日: 2006-07-22, 公開日: 2006-10-18, 最終更新日: 2023-12-13)

主引用文献

Hartmann, M.D.,Bourenkov, G.P.,Oberschall, A.,Strizhov, N.,Bartunik, H.D.
Mechanism of Phosphoryl Transfer Catalyzed by Shikimate Kinase from Mycobacterium Tuberculosis.
J.Mol.Biol., 364:411-, 2006

PubMed Abstract: The structural mechanism of the catalytic functioning of shikimate kinase from Mycobacterium tuberculosis was investigated on the basis of a series of high-resolution crystal structures corresponding to individual steps in the enzymatic reaction. The catalytic turnover of shikimate and ATP into the products shikimate-3-phosphate and ADP, followed by release of ADP, was studied in the crystalline environment. Based on a comparison of the structural states before initiation of the reaction and immediately after the catalytic step, we derived a structural model of the transition state that suggests that phosphoryl transfer proceeds with inversion by an in-line associative mechanism. The random sequential binding of shikimate and nucleotides is associated with domain movements. We identified a synergic mechanism by which binding of the first substrate may enhance the affinity for the second substrate.

PubMed: 17020768
DOI: 10.1016/J.JMB.2006.09.001

実験手法

X-RAY DIFFRACTION (1.85 Å)