6U9D

Saccharomyces cerevisiae acetohydroxyacid synthase

6U9D の概要

• エントリーDOI: 10.2210/pdb6u9d/pdb
• 分子名称: Acetolactate synthase catalytic subunit, mitochondrial, Acetolactate synthase small subunit, mitochondrial, THIAMINE DIPHOSPHATE, ... (8 entities in total)
• 機能のキーワード: ahas, pyruvate, fad, dioxygen, transferase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 1261925.03

構造登録者

Guddat, L.W.,Lonhienne, T. (登録日: 2019-09-08, 公開日: 2020-07-15, 最終更新日: 2023-10-11)

主引用文献

Lonhienne, T.,Low, Y.S.,Garcia, M.D.,Croll, T.,Gao, Y.,Wang, Q.,Brillault, L.,Williams, C.M.,Fraser, J.A.,McGeary, R.P.,West, N.P.,Landsberg, M.J.,Rao, Z.,Schenk, G.,Guddat, L.W.
Structures of fungal and plant acetohydroxyacid synthases.
Nature, 586:317-321, 2020

PubMed Abstract: Acetohydroxyacid synthase (AHAS), also known as acetolactate synthase, is a flavin adenine dinucleotide-, thiamine diphosphate- and magnesium-dependent enzyme that catalyses the first step in the biosynthesis of branched-chain amino acids. It is the target for more than 50 commercial herbicides. AHAS requires both catalytic and regulatory subunits for maximal activity and functionality. Here we describe structures of the hexadecameric AHAS complexes of Saccharomyces cerevisiae and dodecameric AHAS complexes of Arabidopsis thaliana. We found that the regulatory subunits of these AHAS complexes form a core to which the catalytic subunit dimers are attached, adopting the shape of a Maltese cross. The structures show how the catalytic and regulatory subunits communicate with each other to provide a pathway for activation and for feedback inhibition by branched-chain amino acids. We also show that the AHAS complex of Mycobacterium tuberculosis adopts a similar structure, thus demonstrating that the overall AHAS architecture is conserved across kingdoms.

PubMed: 32640464
DOI: 10.1038/s41586-020-2514-3

実験手法

X-RAY DIFFRACTION (3.194 Å)