2F1F

Crystal structure of the regulatory subunit of acetohydroxyacid synthase isozyme III from E. coli

2F1F の概要

• エントリーDOI: 10.2210/pdb2f1f/pdb
• 分子名称: Acetolactate synthase isozyme III small subunit, MAGNESIUM ION, PENTAETHYLENE GLYCOL, ... (5 entities in total)
• 機能のキーワード: ferredoxin fold, act domain, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 36854.16

構造登録者

Kaplun, A.,Vyazmensky, M.,Barak, Z.,Chipman, D.M.,Shaanan, B. (登録日: 2005-11-14, 公開日: 2006-01-24, 最終更新日: 2024-02-14)

主引用文献

Kaplun, A.,Vyazmensky, M.,Zherdev, Y.,Belenky, I.,Slutzker, A.,Mendel, S.,Barak, Z.,Chipman, D.M.,Shaanan, B.
Structure of the Regulatory Subunit of Acetohydroxyacid Synthase Isozyme III from Escherichia coli.
J.Mol.Biol., 357:951-963, 2006

PubMed Abstract: The enzyme acetohydroxyacid synthase (AHAS) catalyses the first common step in the biosynthesis of the three branched-chain amino acids. Enzymes in the AHAS family generally consist of regulatory and catalytic subunits. Here, we describe the first crystal structure of an AHAS regulatory subunit, the ilvH polypeptide, determined at a resolution of 1.75 A. IlvH is the regulatory subunit of one of three AHAS isozymes expressed in Escherichia coli, AHAS III. The protein is a dimer, with two beta alpha beta beta alpha beta ferredoxin domains in each monomer. The two N-terminal domains assemble to form an ACT domain structure remarkably close to the one predicted by us on the basis of the regulatory domain of 3-phosphoglycerate dehydrogenase (3PGDH). The two C-terminal domains combine so that their beta-sheets are roughly positioned back-to-back and perpendicular to the extended beta-sheet of the N-terminal ACT domain. On the basis of the properties of mutants and a comparison with 3PGDH, the effector (valine) binding sites can be located tentatively in two symmetrically related positions in the interface between a pair of N-terminal domains. The properties of mutants of the ilvH polypeptide outside the putative effector-binding site provide further insight into the functioning of the holoenzyme. The results of this study open avenues for further studies aimed at understanding the mechanism of regulation of AHAS by small-molecule effectors.

PubMed: 16458324
DOI: 10.1016/j.jmb.2005.12.077

実験手法

X-RAY DIFFRACTION (1.75 Å)