Structure of free fumarase C from Escherichia coli

Weaver T

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Structure of free fumarase C from Escherichia coli

机译：延胡索酸酶C从大肠杆菌的结构

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Previous crystal structures of fumarase C from Escherichia coli have noted two occupied dicarboxylate-binding sites termed the active site and the B site. Here, the first known fumarase C structure is reported in which both sites are unoccupied by bound ligand. This so-called 'free' crystal form shows conservation of the active-site water in a similar orientation to that reported in other fumarase C crystal structures. More importantly, a shift of His129 has been observed at the B site. This new crystallographic information suggests the use of water as a permanent member of the active site and the use of an imidazole-imidazolium conversion to control access at the allosteric B site.

机译：延胡索酸酶C的晶体结构大肠杆菌有提到两个占领dicarboxylate-binding网站称为活动网站和网站。延胡索酸酶C结构的报道网站由绑定空置的配体。所谓的“免费”水晶形式显示保护活性部位的水在一个类似的取向与其他报告延胡索酸酶C晶体结构。已经观察到B网站。建议使用晶体信息水作为常任理事国活性部位和imidazole-imidazolium的使用转换控制访问的变构B网站。

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《Acta crystallographica.Section D. Biological crystallography》 |2005年第10期|1395-1401|共7页
作者
Weaver T;
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作者单位

Univ Wisconsin, Dept Chem, La Crosse, WI 54601 USA;

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原文格式 PDF
正文语种英语
中图分类化学;
关键词
Histidine; Escherichia coli; Mutantscrystal structureMutationproton transportWater utilizationcrystal outlineActive Site;

机译：组氨酸;大肠杆菌;MutantscrystalstructureMutationproton transportWaterutilizationcrystal outlineActive网站;

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Structure of free fumarase C from Escherichia coli

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