Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 470, Issue 1, Pages 88-93Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2015.12.123
Keywords
beta-barrel structure; Fatty acid-binding protein; Catalytic site; Dinoflagellate luciferase; Coelenterazine analogs
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Funding
- JSPS KAKENHI Grant [26560443]
- MEXT, Japan
- AMED, Japan
- Grants-in-Aid for Scientific Research [26560443] Funding Source: KAKEN
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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 angstrom resolution. The structure consists of 11 antiparallel beta-strands forming a beta-barrel that is capped by 4 short alpha-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 beta-barrel structure. (C) 2015 Elsevier Inc. All rights reserved.
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