OLD YELLOW ENZYME AT 2-ANGSTROM RESOLUTION - OVERALL STRUCTURE, LIGAND-BINDING, AND COMPARISON WITH RELATED FLAVOPROTEINS
OLD YELLOW ENZYME AT 2-ANGSTROM RESOLUTION - OVERALL STRUCTURE, LIGAND-BINDING, AND COMPARISON WITH RELATED FLAVOPROTEINS
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DOI：
10.1016/s0969-2126(94)00111-1
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发表时间：
1994-11-15
期刊：
影响因子：
5.7
通讯作者：
KARPLUS, PA
中科院分区：
文献类型：
--
作者：
FOX, KM;KARPLUS, PA
老黄酶（OYE）是第一个被纯化的黄素酶，但其功能尚不清楚。尽管如此，NADPH氧化酶活性，黄素单核苷酸环境和OYE的配体结合特性已被广泛研究的生化和光谱方法。这些数据的充分解释需要结构informations.Results：在2埃分辨率的氧化和还原OYE的晶体结构揭示了一个α/β桶拓扑结构清楚地与三甲胺脱氢酶。OYE与对羟基苯甲醛、β-雌二醇和NADPH类似物的复合物显示所有三种结合在共同位点，堆叠在黄素上。假定的NADPH结合模式是新颖的，因为它涉及到的烟酰胺montettide portion.Conclusions的主要识别：这项工作表明，显着的光谱变化后看到苯酚结合是由于密切的物理协会的黄素和酚。它还确定了OYE的结构类别，并表明如果NADPH是其真正的底物，那么OYE在进化过程中采用了NADPH依赖性。
Old yellow enzyme (OYE) was the first flavoenzyme purified, but its function is still unknown. Nevertheless, the NADPH oxidase activity, the flavin mononucleotide environment and the ligand-binding properties of OYE have been extensively studied by biochemical and spectroscopic approaches. Full interpretation of these data requires structural information.Results: The crystal structures of oxidized and reduced OYE at 2 Angstrom resolution reveal an alpha/beta-barrel topology clearly related to trimethylamine dehydrogenase. Complexes of OYE with p-hydroxybenzaldehyde, beta-estradiol, and an NADPH analog show all three binding at a common site, stacked on the flavin. The putative NADPH binding mode is novel as it involves primary recognition of the nicotinamide mononucleotide portion.Conclusions: This work shows that the striking spectral changes seen upon phenol binding are due to close physical association of the flavin and phenolate. It also identifies the structural class of OYE and suggests that if NADPH is its true substrate, then OYE has adopted NADPH dependence during evolution.