荧光素酶
生物发光
荧光素
反平行(数学)
化学
光蛋白
晶体结构
阿奎林
生物化学
立体化学
结晶学
细胞内
基因
磁场
量子力学
物理
转染
作者
Yuri Tomabechi,Takamitsu Hosoya,Haruhiko Ehara,Shun-ichi Sekine,Mikako Shirouzu,Satoshi Inouye
标识
DOI:10.1016/j.bbrc.2015.12.123
摘要
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.
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