1N1Z

(+)-Bornyl Diphosphate Synthase: Complex with Mg and pyrophosphate

1N1Z の概要

• エントリーDOI: 10.2210/pdb1n1z/pdb
• 関連するPDBエントリー: 1N1B 1N20 1N21 1N22 1N23 1N24
• 分子名称: (+)-bornyl diphosphate synthase, MAGNESIUM ION, 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (5 entities in total)
• 機能のキーワード: terpene synthase fold, isomerase
• 由来する生物種: Salvia officinalis (garden sage)
• 細胞内の位置: Plastid, chloroplast: O81192
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 128987.56

構造登録者

Whittington, D.A.,Wise, M.L.,Urbansky, M.,Coates, R.M.,Croteau, R.B.,Christianson, D.W. (登録日: 2002-10-21, 公開日: 2002-11-27, 最終更新日: 2024-02-14)

主引用文献

Whittington, D.A.,Wise, M.L.,Urbansky, M.,Coates, R.M.,Croteau, R.B.,Christianson, D.W.
Bornyl diphosphate synthase: Structure and strategy for carbocation manipulation by a terpenoid cyclase
Proc.Natl.Acad.Sci.USA, 99:15375-15380, 2002

PubMed Abstract: The x-ray crystal structure of dimeric (+)-bornyl diphosphate synthase, a metal-requiring monoterpene cyclase from Salvia officinalis, is reported at 2.0-A resolution. Each monomer contains two alpha-helical domains: the C-terminal domain catalyzes the cyclization of geranyl diphosphate, orienting and stabilizing multiple reactive carbocation intermediates; the N-terminal domain has no clearly defined function, although its N terminus caps the active site in the C-terminal domain during catalysis. Structures of complexes with aza analogues of substrate and carbocation intermediates, as well as complexes with pyrophosphate and bornyl diphosphate, provide "snapshots" of the terpene cyclization cascade.

PubMed: 12432096
DOI: 10.1073/pnas.232591099

実験手法

X-RAY DIFFRACTION (2.3 Å)