1brl
THREE-DIMENSIONAL STRUCTURE OF BACTERIAL LUCIFERASE FROM VIBRIO HARVEYI AT 2.4 ANGSTROMS RESOLUTION
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OverviewOverview
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.
About this StructureAbout this Structure
1BRL is a Protein complex structure of sequences from Vibrio harveyi with as ligand. The following page contains interesting information on the relation of 1BRL with [Luciferase]. Active as Alkanal monooxygenase (FMN-linked), with EC number 1.14.14.3 Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4 A resolution., Fisher AJ, Raushel FM, Baldwin TO, Rayment I, Biochemistry. 1995 May 23;34(20):6581-6. PMID:7756289
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