1BRL

THREE-DIMENSIONAL STRUCTURE OF BACTERIAL LUCIFERASE FROM VIBRIO HARVEYI AT 2.4 ANGSTROMS RESOLUTION

1BRL の概要

• エントリーDOI: 10.2210/pdb1brl/pdb
• 分子名称: BACTERIAL LUCIFERASE, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: monooxygenase, luminescence
• 由来する生物種: Vibrio harveyi; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 153258.46

構造登録者

Fisher, A.J.,Rayment, I. (登録日: 1995-03-20, 公開日: 1996-04-01, 最終更新日: 2024-02-07)

主引用文献

Fisher, A.J.,Raushel, F.M.,Baldwin, T.O.,Rayment, I.
Three-dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4 A resolution.
Biochemistry, 34:6581-6586, 1995

PubMed Abstract: Luciferases are a class of enzymes that generate light in the visible spectrum. Luciferase from luminous marine bacteria is an alpha-beta heterodimer monooxygenase that catalyzes the oxidation of FMNH2 and a long-chain aliphatic aldehyde. The X-ray crystal structure of bacterial luciferase from Vibrio harveyi has been determined to 2.4 A resolution. The structure was solved by a combination of multiple isomorphous replacement and molecular averaging between the two heterodimers in the asymmetric unit. Each subunit folds into a (beta/alpha)8 barrel motif, and dimerization is mediated through a parallel four-helix bundle centered on a pseudo 2-fold axis that relates the structurally similar subunits. The vicinity of the active site has been identified on the alpha subunit by correlations with similar protein motifs and previous biochemical studies. The structure presented here represents the first molecular model of a bioluminescent enzyme.

PubMed: 7756289
DOI: 10.1021/bi00020a002

実験手法

X-RAY DIFFRACTION (2.4 Å)