1DS0

CRYSTAL STRUCTURE OF CLAVAMINATE SYNTHASE

1DS0 の概要

• エントリーDOI: 10.2210/pdb1ds0/pdb
• 関連するPDBエントリー: 1DRT 1DRY 1DS1
• 分子名称: CLAVAMINATE SYNTHASE 1, ACETATE ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: oxygenase, trifunctional enzyme, clavaminate synthase 1, jelly roll, oxidoreductase, lyase
• 由来する生物種: Streptomyces clavuligerus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35763.02

構造登録者

Zhang, Z.H.,Ren, J.,Stammers, D.K.,Baldwin, J.E.,Harlos, K.,Schofield, C.J. (登録日: 2000-01-06, 公開日: 2000-07-06, 最終更新日: 2024-02-07)

主引用文献

Zhang, Z.,Ren, J.,Stammers, D.K.,Baldwin, J.E.,Harlos, K.,Schofield, C.J.
Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase.
Nat.Struct.Biol., 7:127-133, 2000

PubMed Abstract: Clavaminate synthase (CAS), a remarkable Fe(II)/2-oxoglutarate oxygenase, catalyzes three separate oxidative reactions in the biosynthesis of clavulanic acid, a clinically used inhibitor of serine beta-lactamases. The first CAS-catalyzed step (hydroxylation) is separated from the latter two (oxidative cyclization/desaturation) by the action of an amidinohydrolase. Here, we describe crystal structures of CAS in complex with Fe(II), 2-oxoglutarate (2OG) and substrates (N-alpha-acetyl-L-arginine and proclavaminic acid). They reveal how CAS catalyzes formation of the clavam nucleus, via a process unprecedented in synthetic organic chemistry, and suggest how it discriminates between substrates and controls reaction of its highly reactive ferryl intermediate. The presence of an unpredicted jelly roll beta-barrel core in CAS implies divergent evolution within the family of 2OG and related oxygenases. Comparison with other non-heme oxidases/oxygenases reveals flexibility in the position which dioxygen ligates to the iron, in contrast to the analogous heme-using enzymes.

PubMed: 10655615
DOI: 10.1038/72398

実験手法

X-RAY DIFFRACTION (1.63 Å)