WrbA连接细菌黄素氧还蛋白和真核生物NAD(P)H:醌氧化还原酶。
WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases.
作者信息
Carey Jannette, Brynda Jiri, Wolfová Julie, Grandori Rita, Gustavsson Tobias, Ettrich Rüdiger, Smatanová Ivana Kutá
机构信息
Chemistry Department, Princeton University, Princeton, New Jersey 08544-1009, USA.
出版信息
Protein Sci. 2007 Oct;16(10):2301-5. doi: 10.1110/ps.073018907.
Abstract
The crystal structure of the flavodoxin-like protein WrbA with oxidized FMN bound reveals a close relationship to mammalian NAD(P)H:quinone oxidoreductase, Nqo1. Structural comparison of WrbA, flavodoxin, and Nqo1 indicates how the twisted open-sheet fold of flavodoxins is elaborated to form multimers that extend catalytic function from one-electron transfer between protein partners using FMN to two-electron reduction of xenobiotics using FAD. The structure suggests a novel physiological role for WrbA and Nqo1.
摘要
结合氧化型黄素单核苷酸（FMN）的类黄素氧还蛋白WrbA的晶体结构显示出其与哺乳动物烟酰胺腺嘌呤二核苷酸磷酸（NAD(P)H）：醌氧化还原酶Nqo1的密切关系。WrbA、黄素氧还蛋白和Nqo1的结构比较表明，黄素氧还蛋白扭曲的开放片层折叠是如何进一步形成多聚体的，这种多聚体将催化功能从利用FMN在蛋白质伙伴之间进行单电子转移扩展到利用黄素腺嘌呤二核苷酸（FAD）对外源生物进行双电子还原。该结构表明了WrbA和Nqo1的一种新的生理作用。
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