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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >The organization of divalent cations in the active site of cadmium Escherichia coli fructose-1,6-bisphosphate aldolase.
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The organization of divalent cations in the active site of cadmium Escherichia coli fructose-1,6-bisphosphate aldolase.

机译：二价阳离子的组织活动镉的大肠杆菌的特性,6-bisphosphate醛缩酶。

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摘要

Previously determined crystal structures of the zinc enzyme Escherichia coli class II fructose-1,6-bisphosphate aldolase display good agreement for the protein structure but a differing metal-ion organization in the active site. The structure of the enzyme with Cd(2+) in place of Zn(2+) has now been determined to 2.0 A resolution to facilitate cation identification. The protein structure was essentially identical to other structures and five Cd(2+) positions were identified. Two of the cations are at the active site; one corresponds to the catalytic ion and the other provides a structural contribution. These Cd(2+) sites are equivalent to two Zn(2+) ions observed when the enzyme is complexed with a transition-state mimic and confirm our assignment of the roles played by these ions.
机译：以前的晶体结构决定的锌酶大肠杆菌类II的特性,6-bisphosphate醛缩酶显示良好但协议的蛋白质结构不同的金属离子组织活跃网站。锌(2 +)的地方现在已经决心2.0解决促进阳离子识别。蛋白质结构本质上是相同的其他结构和五个Cd(2 +)的位置被确定。活性部位;另提供一个结构的贡献。这些Cd(2 +)网站相当于两个锌(2 +)离子观察当酶包裹着过渡态模拟和确认我们的作业这些离子所扮演的角色。

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