Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10749349 | Biochemical and Biophysical Research Communications | 2016 | 6 Pages |
Abstract
The 19Â 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 19Â kDa protein (nanoKAZ) was determined at 1.71Â Ã
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.
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Authors
Yuri Tomabechi, Takamitsu Hosoya, Haruhiko Ehara, Shun-ichi Sekine, Mikako Shirouzu, Satoshi Inouye,