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首页> 外文期刊>Journal of Molecular Biology >CRYSTAL STRUCTURE OF CYTOPLASMIC ESCHERICHIA COLI PEPTIDYL-PROLYL ISOMERASE - EVIDENCE FOR DECREASED MOBILITY OF LOOPS UPON COMPLEXATION
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CRYSTAL STRUCTURE OF CYTOPLASMIC ESCHERICHIA COLI PEPTIDYL-PROLYL ISOMERASE - EVIDENCE FOR DECREASED MOBILITY OF LOOPS UPON COMPLEXATION

机译：胞质大肠埃希菌肽-脯氨酸异构酶的晶体结构-环的复杂性降低的证据。

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摘要

The structure of the unliganded form of the Escherichia coil cytoplasmic peptidyl-prolyl isomerase (ppiB gene product) in a new crystal form was determined by the molecular replacement method and refined to an R-factor of 16.1% at 2.1 Angstrom resolution. The enzyme crystallized in the orthorhombic C222(1) space group with unit cell dimensions of a = 44.7 Angstrom, b = 68.2 Angstrom and c = 102.0 Angstrom. Comparison with the reported structure of the enzyme complexed with the tripeptide substrate succinyl-Ala-Pro-Ala-p-nitroanilide revealed subtle changes that occur upon complex formation. There is evidence to suggest that two surface loops have significantly reduced mobility in the complexed structure. (C) Academic Press Limited. [References: 32]
机译：通过分子置换法确定新晶体形式的大肠杆菌线圈胞质肽基-脯氨酰异构酶（ppiB基因产物）的非配体形式的结构，并在2.1埃分辨率下将其精制至16.1％的R因子。该酶在正交晶C222（1）空间群中结晶，其晶胞尺寸为a = 44.7埃，b = 68.2埃和c = 102.0埃。与报道的与三肽底物琥珀酰-Ala-Pro-Ala-对硝基苯胺络合的酶结构的比较表明，在形成复合物时会发生细微的变化。有证据表明，两个表面环在复杂结构中的迁移率大大降低。 （C）学术出版社有限公司。 [参考：32]

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