Three-dimensional structure of bacterial luciferase from vibrio harveyi at 2.4 Å resolution 1,2

Research output: Contribution to journalArticle

101 Scopus citations

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 Å 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 (β/α)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.

Original languageEnglish (US)
Pages (from-to)6581-6586
Number of pages6
JournalBiochemistry®
Volume34
Issue number20
StatePublished - 1995
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'Three-dimensional structure of bacterial luciferase from vibrio harveyi at 2.4 Å resolution 1,2'. Together they form a unique fingerprint.

  • Cite this