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首页> 外文期刊>FEBS letters. >Crystal structure of a NADPH NADPH ‐cytochrome P450 oxidoreductase ( CYPOR CYPOR ) and heme oxygenase 1 fusion protein implies a conformational change in CYPOR CYPOR upon NADPH NADPH / NADP NADP + + binding
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Crystal structure of a NADPH NADPH ‐cytochrome P450 oxidoreductase ( CYPOR CYPOR ) and heme oxygenase 1 fusion protein implies a conformational change in CYPOR CYPOR upon NADPH NADPH / NADP NADP + + binding

机译：NADPH NADPH -COYCOCHROME P450氧化酶（CYPOR CYPOR）和血红素氧酶1融合蛋白的晶体结构意味着CYPOR CYPOR在NADPH NADPH / NADP NADP + +绑定时的构象变化

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摘要

Heme oxygenase‐1 ( HMOX 1) catalyzes heme degradation utilizing reducing equivalents supplied from NADPH ‐cytochrome P450 reductase ( CYPOR ). Recently, we determined the complex structure of NADP + ‐bound open‐conformation stabilized CYPOR and heme‐ HMOX 1, but the resolution was limited to 4.3 ?. Here, we determined the crystal structure of the fusion protein of open‐conformation stabilized CYPOR and heme‐ HMOX 1 at 3.25 ? resolution. Unexpectedly, no NADP + was bound to this fusion protein in the crystal. Structural comparison of the NADP + ‐bound complex and the NADP + ‐free fusion protein suggests that NADP + binding regulates the conformational change in the FAD ‐binding domain of CYPOR . As a result of this change, the FMN ‐binding domain of CYPOR approaches heme‐bound HMOX 1 upon NADP + binding to enhance the electron‐transfer efficiency from FMN to heme.
机译：血红素氧合酶-1（HMOX 1）催化利用从NADPH -COTCOCHROME P450还原酶（CYPOR）提供的还原等同物的血红液降解。 最近，我们确定了NADP + -Bound开放构象的复杂结构稳定的Cypor和Heme-HMox1，但分辨率限制在4.3？。 在这里，我们确定了3.25的稳定性Cypor和血红素1的融合蛋白的晶蛋白的晶体结构？ 解析度。 出乎意料的是，没有NADP +在晶体中含有该融合蛋白。 NADP + -BOUND复合物和NADP + -FREE融合蛋白的结构比较表明NADP +结合调节CYPOR的FAD耦合结构域的构象变化。 由于这种变化，CYPOR的FMN粘接结构域在NADP +结合时接近血红结HMOX1，以增强来自FMN至血红素的电子转移效率。

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