4GO5

The regulatory subunit of aspartate kinase from Mycobacterium tuberculosis

4GO5 の概要

• エントリーDOI: 10.2210/pdb4go5/pdb
• 関連するPDBエントリー: 4GO7
• 分子名称: Aspartokinase (2 entities in total)
• 機能のキーワード: transferase
• 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: 21502.20

構造登録者

Yang, Q.,Li, X. (登録日: 2012-08-18, 公開日: 2012-09-05, 最終更新日: 2024-02-28)

主引用文献

Yang, Q.,Yu, K.,Yan, L.,Li, Y.,Chen, C.,Li, X.
Structural view of the regulatory subunit of aspartate kinase from Mycobacterium tuberculosis.
Protein Cell, 2:745-754, 2011

PubMed Abstract: The aspartate kinase (AK) from Mycobacterium tuberculosis (Mtb) catalyzes the biosynthesis of aspartate family amino acids, including lysine, threonine, isoleucine and methionine. We determined the crystal structures of the regulatory subunit of aspartate kinase from Mtb alone (referred to as MtbAKβ) and in complex with threonine (referred to as MtbAKβ-Thr) at resolutions of 2.6 Å and 2.0 Å, respectively. MtbAKβ is composed of two perpendicular non-equivalent ACT domains [aspartate kinase, chorismate mutase, and TyrA (prephenate dehydrogenase)] per monomer. Each ACT domain contains two α helices and four antiparallel β strands. The structure of MtbAKβ shares high similarity with the regulatory subunit of the aspartate kinase from Corynebacterium glutamicum (referred to as CgAKβ), suggesting similar regulatory mechanisms. Biochemical assays in our study showed that MtbAK is inhibited by threonine. Based on crystal structure analysis, we discuss the regulatory mechanism of MtbAK.

PubMed: 21976064
DOI: 10.1007/s13238-011-1094-2

実験手法

X-RAY DIFFRACTION (2.6 Å)