Crystal structure of the short-chain flavin reductase HpaC from Sulfolobus tokodaii strain 7

被引：0
|
作者：
Okai, M [1 ]
Kudo, N [1 ]
Nagata, K [1 ]
Lee, WC [1 ]
Kamo, M [1 ]
Tanokura, M [1 ]
机构：
[1] Univ Tokyo, Grad Sch Agr & Life Sci, Bunkyo Ku, Tokyo 1138657, Japan
来源：
PROCEEDINGS OF THE JAPAN ACADEMY SERIES B-PHYSICAL AND BIOLOGICAL SCIENCES | 2005年 / 81卷 / 06期
关键词：
short-chain flavin reductase; HpaC; three-dimensional structure; NADH;
D O I：
10.2183/pjab.81.229
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
Flavin reductases (FRs) catalyze the reduction of free flavins using NADH or NADPH. In recent years, a new family of short-chain FRs have been identified in a variety of bacteria and archaea. Here we have determined the crystal structure of an archaeal short-chain FR, HpaC from an aerobic thermoacidophilic crenarchaeon Sufolobus tokodaii strain 7. The HpaC molecule exists as a homodimer with one FMN for each monomer. On the other hand, PheA2, the most structurally similar protein to HpaC, contains FAD rather than FMN. Structural comparison of these proteins has revealed that the short loop at residues 82-83 and the successive eta 1 helix in HpaC are closer to the bound flavin than those in PheA2. As a result, there is not sufficient space to accommodate the AMP moiety of FAD in HpaC, and thus HpaC prefers FMN to FAD.
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收藏
页码：229 / 232
页数：4
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