Crystal structure of nanoKAZ: The mutated 19 kDa component of Oplophorus luciferase catalyzing the bioluminescent reaction with coelenterazine

Biochem Biophys Res Commun. 2016 Jan 29;470(1):88-93. doi: 10.1016/j.bbrc.2015.12.123. Epub 2015 Dec 30.

Abstract

The 19 kDa protein (KAZ) of Oplophorus luciferase is a catalytic component, that oxidizes coelenterazine (a luciferin) with molecular oxygen to emit light. The crystal structure of the mutated 19 kDa protein (nanoKAZ) was determined at 1.71 Å resolution. The structure consists of 11 antiparallel β-strands forming a β-barrel that is capped by 4 short α-helices. The structure of nanoKAZ is similar to those of fatty acid-binding proteins (FABPs), even though the amino acid sequence similarity was very low between them. The coelenterazine-binding site and the catalytic site for the luminescence reaction might be in a central cavity of the β-barrel structure.

Keywords: Catalytic site; Coelenterazine analogs; Dinoflagellate luciferase; Fatty acid-binding protein; β-barrel structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arthropod Proteins / chemistry*
  • Arthropod Proteins / ultrastructure*
  • Binding Sites
  • Catalysis
  • Computer Simulation
  • Crustacea / enzymology*
  • Imidazoles / chemistry*
  • Luciferases / chemistry*
  • Luciferases / ultrastructure*
  • Luminescent Measurements / methods
  • Luminescent Proteins / chemistry
  • Luminescent Proteins / therapeutic use
  • Models, Chemical
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Tertiary
  • Pyrazines / chemistry*

Substances

  • Arthropod Proteins
  • Imidazoles
  • Luminescent Proteins
  • Pyrazines
  • coelenterazine
  • Luciferases