Structural and dynamic implications of an effector-induced backbone amide cis-trans isomerization in cytochrome P450cam.
Structural and dynamic implications of an effector-induced backbone amide cis-trans isomerization in cytochrome P450cam.
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DOI：
10.1016/j.jmb.2009.03.046
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发表时间：
2009-05-15
影响因子：
5.6
通讯作者：
Pochapsky, Thomas C.
中科院分区：
文献类型：
--
作者：
Asciutto, Eliana K.;Madura, Jeffry D.;Pochapsky, Susan Sondej;OuYang, Bo;Pochapsky, Thomas C.
实验结果表明，细胞色素P450 cam（CYP 101）中Ile 88-Pro 89肽键的顺-反异构化具有功能相关性。异构化被认为是导致CYP 101在与效应蛋白putidaredoxin（Pdx）结合后形成催化活性形式的结构重组的关键因素。的顺式和反式构象的底物和碳一氧结合亚铁CYP 101与序列特异性的Pdx诱导的结构扰动的核磁共振的分子动力学模拟的结果的详细比较，提供洞察异构化的结构和动力学后果。Pdx结合位点的近端面的CYP 101和异构化的网站之间的机械耦合进行了描述。
Experimental evidence has been provided for a functionally relevant cis-trans isomerization of the Ile 88-Pro 89 peptide bond in cytochrome P450cam (CYP101). The isomerization is proposed to be a key element of the structural reorganization leading to the catalytically competent form of CYP101 upon binding of the effector protein putidaredoxin (Pdx). A detailed comparison of the results of molecular dynamics simulations on the cis and trans conformations of substrate- and carbonmonoxy-bound ferrous CYP101 with sequence-specific Pdx-induced structural perturbations identified by nuclear magnetic resonance is presented, providing insight into the structural and dynamic consequences of the isomerization. The mechanical coupling between the Pdx binding site on the proximal face of CYP101 and the site of isomerization is described.
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