Crystal structure of nanoKAZ: The mutated 19 kDa component of Oplophorus luciferase catalyzing the bioluminescent reaction with coelenterazine

被引：42

作者：

Tomabechi, Yuri ^{[1
]}

Hosoya, Takamitsu ^{[2
]}

Ehara, Haruhiko ^{[1
]}

Sekine, Shun-ichi ^{[1
]}

Shirouzu, Mikako ^{[1
]}

Inouye, Satoshi ^{[3
]}

机构：

[1] RIKEN Ctr Life Sci Technol, Div Struct & Synthet Biol, Tsurumi Ku, 1-7-22 Suehiro Cho, Yokohama, Kanagawa 2300045, Japan

[2] Tokyo Med & Dent Univ, Inst Biomat & Bioengn, Lab Chem Biosci, Chiyoda Ku, 2-3-10 Kanda Surugadai, Tokyo 1010062, Japan

[3] JNC Co, Yokohama Res Ctr, Kanazawa Ku, 5-1 Okawa, Yokohama, Kanagawa 2368605, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2016年 / 470卷 / 01期

关键词：

beta-barrel structure; Fatty acid-binding protein; Catalytic site; Dinoflagellate luciferase; Coelenterazine analogs; DEEP-SEA SHRIMP; PROTEIN; LUMINESCENCE; RENILLA; PURIFICATION; EXPRESSION; SUBSTRATE; REPORTER; ANALOGS; SYSTEM;

D O I：

10.1016/j.bbrc.2015.12.123

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 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.

引用

页码：88 / 93

页数：6

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