| Literature DB >> 26746005 |
Yuri Tomabechi1, Takamitsu Hosoya2, Haruhiko Ehara1, Shun-Ichi Sekine1, Mikako Shirouzu1, Satoshi Inouye3.
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.Entities:
Keywords: Catalytic site; Coelenterazine analogs; Dinoflagellate luciferase; Fatty acid-binding protein; β-barrel structure
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Year: 2015 PMID: 26746005 DOI: 10.1016/j.bbrc.2015.12.123
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575