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学科主题: 生命有机化学
题名: X-ray structure of methanol dehydrogenase from paracoccus denitrificans and molecular modeling of its interactions with cytochrome c-551i
其他题名: 从paracoccus denitrificans提取的甲醇脱氢酶的X-射线法测定的结构及其与细胞色素c-551i的相互作用的计算机模拟
作者: Xia ZX(夏宗芗) ; Dai WW(戴伟文) ; He YN(何永宁) ; Scott A. White ; F. Scott Mathews ; Victor L. Davidson
通讯作者: F. Scott Mathews
刊名: J. Biol. Inog. Chem.
发表日期: 2003-01-01T00:00:00Z
卷: 8, 期:8, 页:843-854
收录类别: SCI
部门归属: 中国科学院上海有机化学研究所生命有机化学实验室; California Institute of Technology, Pasadena, CA, 91125 USA; University of Birmingham, Birmingham, B152TT UK
英文摘要: The X-ray structure of methanol dehydroge-nase (MEDH) from Paracgccus denitrificans (MEDH- PD) was determined at 2.5 A resolution using molecularreplacement based on the structure of MEDH from Methylophilus methylotrophus W3A1 (MEDH-WA). The overall structures from the two bacteria are similar to each other except that the former has a longer C-terminal tail in each subunit and shows local differences in several insertion regions. The "X-ray sequence" of the segment αGly444-αLeu452 was established, including one insertion and seven replacements compared with the reported sequence. The primary electron acceptor of MEDH-PD is cytochrome c-55li (Cytc55li). Based on the crystal structure of MEDH-PD and of the published structure of Cytc55li, their interactions were investi-gated by molecular modeling. As a guide and starting point, the covalently attached cytochrome and PQQ domains of the alcohol dehydrogenase from Pseudomo- nas putida HK5 (ADH2B) were used. In the modeling, two molecules of Cytc551i could be accommodated in their interaction with the MEDH heterotetramer in accordance with the two-fold molecular symmetry of the latter. Two models are proposed, in both of which major contributions to inter-protein binding. One of these models involves salt bridges from αArg99 of MEDH to the heme propionic acids of Cytc55li and the other involves salt bridges from αArg426 of MEDH to Glull2 of Cytc55li. Both involve salt bridges from αLys93 of MEDH to Asp75 of Cytc55li. The size and nature of the cytochrome/quinoprotein heterodimer interfaces and calculations of electronic coupling and electron transfer rates favor one of these models over the other.
语种: 英语
相关网址: 查看原文
内容类型: 期刊论文
URI标识: http://ir.sioc.ac.cn/handle/331003/23684
Appears in Collections:生命有机化学国家重点实验室_期刊论文

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Recommended Citation:
Xia ZX,Dai WW,He YN,et al. X-ray structure of methanol dehydrogenase from paracoccus denitrificans and molecular modeling of its interactions with cytochrome c-551i[J]. J. Biol. Inog. Chem.,2003,8(8):843-854.
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