期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 470, 期 1, 页码 88-93出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2015.12.123
关键词
beta-barrel structure; Fatty acid-binding protein; Catalytic site; Dinoflagellate luciferase; Coelenterazine analogs
资金
- JSPS KAKENHI Grant [26560443]
- MEXT, Japan
- AMED, Japan
- Grants-in-Aid for Scientific Research [26560443] Funding Source: KAKEN
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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