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

Research output: Contribution to journalArticle

99 Citations (Scopus)

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

Fingerprint

Bacterial Luciferases
Vibrio
Luciferases
Amino Acid Motifs
Molecular Models
Dimerization
Enzymes
Mixed Function Oxygenases
Aldehydes
Catalytic Domain
Bacteria
Crystal structure
X-Rays
Light
X rays
Oxidation
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Three-dimensional structure of bacterial luciferase from vibrio harveyi at 2.4 Å resolution 1,2. / Fisher, Andrew J.

In: Biochemistry®, Vol. 34, No. 20, 1995, p. 6581-6586.

Research output: Contribution to journalArticle

@article{657e598450c5458191a9d6701814c044,
title = "Three-dimensional structure of bacterial luciferase from vibrio harveyi at 2.4 {\AA} resolution 1,2",
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 {\AA} 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.",
author = "Fisher, {Andrew J}",
year = "1995",
language = "English (US)",
volume = "34",
pages = "6581--6586",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "20",

}

TY - JOUR

T1 - Three-dimensional structure of bacterial luciferase from vibrio harveyi at 2.4 Å resolution 1,2

AU - Fisher, Andrew J

PY - 1995

Y1 - 1995

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0029027663&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029027663&partnerID=8YFLogxK

M3 - Article

VL - 34

SP - 6581

EP - 6586

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 20

ER -