Tomabechi Yuri, Hosoya Takamitsu, Ehara Haruhiko, Sekine Shun-Ichi, Shirouzu Mikako, Inouye Satoshi
Division of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan.
Laboratory of Chemical Bioscience, Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University, 2-3-10 Kanda-Surugadai, Chiyoda-ku, Tokyo 101-0062, Japan.
Biochem Biophys Res Commun. 2016 Jan 29;470(1):88-93. doi: 10.1016/j.bbrc.2015.12.123. Epub 2015 Dec 30.
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.
萤乌贼荧光素酶的19 kDa蛋白（KAZ）是一种催化成分，它利用分子氧氧化腔肠素（一种荧光素）以发光。突变的19 kDa蛋白（nanoKAZ）的晶体结构在1.71 Å分辨率下得以确定。该结构由11条反平行β链组成，形成一个β桶，由4条短α螺旋封顶。尽管nanoKAZ与脂肪酸结合蛋白（FABP）之间的氨基酸序列相似性很低，但nanoKAZ的结构与FABP的结构相似。腔肠素结合位点和发光反应的催化位点可能位于β桶结构的中央腔内。
