1EBF

HOMOSERINE DEHYDROGENASE FROM S. CEREVISIAE COMPLEX WITH NAD+

1EBF の概要

• エントリーDOI: 10.2210/pdb1ebf/pdb
• 関連するPDBエントリー: 1EBU
• 分子名称: HOMOSERINE DEHYDROGENASE, SODIUM ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total)
• 機能のキーワード: dehydrogenase, dinucleotide, homoserine, nad, dimer, oxidoreductase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 77536.94

構造登録者

DeLaBarre, B.,Thompson, P.R.,Wright, G.D.,Berghuis, A.M. (登録日: 2000-01-24, 公開日: 2000-03-08, 最終更新日: 2024-02-07)

主引用文献

DeLaBarre, B.,Thompson, P.R.,Wright, G.D.,Berghuis, A.M.
Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases.
Nat.Struct.Biol., 7:238-244, 2000

PubMed Abstract: The structure of the antifungal drug target homoserine dehydrogenase (HSD) was determined from Saccharomyces cerevisiae in apo and holo forms, and as a ternary complex with bound products, by X-ray diffraction. The three forms show that the enzyme is a dimer, with each monomer composed of three regions, the nucleotide-binding region, the dimerization region and the catalytic region. The dimerization and catalytic regions have novel folds, whereas the fold of the nucleotide-binding region is a variation on the Rossmann fold. The novel folds impose a novel composition and arrangement of active site residues when compared to all other currently known oxidoreductases. This observation, in conjunction with site-directed mutagenesis of active site residues and steady-state kinetic measurements, suggest that HSD exhibits a new variation on dehydrogenase chemistry.

PubMed: 10700284
DOI: 10.1038/73359

実験手法

X-RAY DIFFRACTION (2.3 Å)