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学科主题: 生命有机化学
题名: Structures of V45E and V45Y mutants and structure comparison of a variety of cytochrome b^5 mutants
其他题名: 细胞色素b5的V45E和V45Y突变体的晶体结构及其一系列突变体的结构的比较
作者: Gan JH(甘建华) ; Wu J(邬键) ; Wang ZQ(王志强) ; Wang YH(王韵华) ; Huang ZX(黄仲贤) ; Xia ZX(夏宗芗)
通讯作者: 夏宗芗
刊名: Acta Crystallogr. Sect. D-Biol. Crystallogr.
发表日期: 2002-01-01
卷: 58, 页:1298-1306
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; 复旦大学
英文摘要: Val45 is a highly conserved residue and a component of the heme-pocket wall of cytochrome b5. The crystal structures of cytochrome b5 mutants V45E and V45Y have been determined at high resolution. Their overall structures were very similar to that of the wild-type protein. However, Val45 of the wild-type protein points towards the heme, but the large side chains of both Glu45 and Tyr45 of the mutants point towards the solvent. A channel is thus opened and the hydrophobicity of the heme pocket is decreased. The rotation of the porphyrin ring and the conformational change of the axial ligand His39 in the V45Y mutant indicated the the microenvironment of the heme is disturbed because of the mutaiton. The binding constants and the electron-transfer rates between cytochrom b5 and cytochrome c decrease owing to the mutation, which can be accounted for by bolecular modeling: the interiron distances increase in order to eliminate the unreasonably close contacts resulting rom the large volumes of the mutated side chains. The influence of the mutations on the redox potentials and protein stability is also discussed. The structures of seven mutants of cytochrom b5 are compared with each other and the effects of these mutations on the protein properties and functions are summarized.
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/331003/23676
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:
Gan JH,Wu J,Wang ZQ,et al. Structures of V45E and V45Y mutants and structure comparison of a variety of cytochrome b^5 mutants[J]. Acta Crystallogr. Sect. D-Biol. Crystallogr.,2002,58:1298-1306.
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