Crystal structure of a new type of NADPH-dependent quinone oxidoreductase (QOR2) from Escherichia coli

被引:23
作者
Kim, In-Kwon [2 ,3 ]
Yim, Hyung-Soon [2 ,3 ]
Kim, Min-Kyu [2 ,3 ]
Kim, Dong-Won [2 ,3 ]
Kim, Young-Min [2 ,3 ]
Cha, Sun-Shin [1 ]
Kang, Sa-Ouk [2 ,3 ]
机构
[1] Korea Ocean Res & Dev Inst, Marine Biotechnol & New Mat Res Div, Ansan 426744, South Korea
[2] Seoul Natl Univ, Biophys Lab, Sch Biol Sci, Seoul 151742, South Korea
[3] Seoul Natl Univ, Inst Microbiol, Seoul 151742, South Korea
关键词
QOR2; NAD(P)H-dependent quinone oxidoreductase; short-chain dehydrogenase/reductase family; transcriptional regulator; carbon metabolism;
D O I
10.1016/j.jmb.2008.04.003
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
Escherichia coli QOR2 [NAD(P)H-dependent quinone oxidoreductase; a ytfG gene product], which catalyzes two-electron reduction of methyl-1,4-benzoquinone, is a new type of quinone-reducing enzyme with distinct primary sequence and oligomeric conformation from previously known quinone oxidoreductases. The crystal structures of native QOR2 and the QOR2-NADPH (nicotinamide adenine dinucleotide phosphate, reduced form) complex reveal that QOR2 consists of two domains (N-domain and C-domain) resembling those of NmrA, a negative transcriptional regulator that belongs to the short-chain dehydrogenase/reductase family. The N-domain, which adopts the Rossmann fold, provides a platform for NADPH binding, whereas the C-domain, which contains a hydrophobic pocket connected to the NADPH-binding site, appears to play important roles in substrate binding. Asn143 near the NADPH-binding site has been identified to be involved in substrate binding and catalysis from structural and mutational analyses. Moreover, compared with wild-type strain, the qor2-overexpressing strain shows growth retardation and remarkable decrease in several enzymes involved in carbon metabolism, suggesting that QOR2 could play some physiological roles in addition to quinone reduction. (C) 2008 Elsevier Ltd. All rights reserved.
引用
收藏
页码:372 / 384
页数:13
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