3AB2

Crystal structure of aspartate kinase from Corynebacterium glutamicum in complex with threonine

3AB2 の概要

• エントリーDOI: 10.2210/pdb3ab2/pdb
• 関連するPDBエントリー: 2DTJ 3AAW 3AB4
• 分子名称: Aspartokinase, THREONINE, ... (4 entities in total)
• 機能のキーワード: aspartate kinase, concerted inhibition, alternative initiation, amino-acid biosynthesis, atp-binding, diaminopimelate biosynthesis, kinase, lysine biosynthesis, nucleotide-binding, transferase
• 由来する生物種: Corynebacterium glutamicum (Brevibacterium flavum); 詳細
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 515253.02

構造登録者

Yoshida, A.,Tomita, T.,Kuzuyama, T.,Nishiyama, M. (登録日: 2009-11-30, 公開日: 2010-06-23, 最終更新日: 2023-11-01)

主引用文献

Yoshida, A.,Tomita, T.,Kuzuyama, T.,Nishiyama, M.
Mechanism of concerted inhibition of {alpha}2{beta}2-type heterooligomeric aspartate kinase from Corynebacterium glutamicum
J.Biol.Chem., 285:27477-27486, 2010

PubMed Abstract: Aspartate kinase (AK) is the first and committed enzyme of the biosynthetic pathway producing aspartate family amino acids, lysine, threonine, and methionine. AK from Corynebacterium glutamicum (CgAK), a bacterium used for industrial fermentation of amino acids, including glutamate and lysine, is inhibited by lysine and threonine in a concerted manner. To elucidate the mechanism of this unique regulation in CgAK, we determined the crystal structures in several forms: an inhibitory form complexed with both lysine and threonine, an active form complexed with only threonine, and a feedback inhibition-resistant mutant (S301F) complexed with both lysine and threonine. CgAK has a characteristic alpha(2)beta(2)-type heterotetrameric structure made up of two alpha subunits and two beta subunits. Comparison of the crystal structures between inhibitory and active forms revealed that binding inhibitors causes a conformational change to a closed inhibitory form, and the interaction between the catalytic domain in the alpha subunit and beta subunit (regulatory subunit) is a key event for stabilizing the inhibitory form. This study shows not only the first crystal structures of alpha(2)beta(2)-type AK but also the mechanism of concerted inhibition in CgAK.

PubMed: 20573952
DOI: 10.1074/jbc.M110.111153

実験手法

X-RAY DIFFRACTION (2.59 Å)