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首页> 外文期刊>Acta crystallographica. Section D, Biological crystallography. >An enzyme captured in two conformational states: crystal structure of S-adenosyl-L-homocysteine hydrolase from Bradyrhizobium elkanii
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An enzyme captured in two conformational states: crystal structure of S-adenosyl-L-homocysteine hydrolase from Bradyrhizobium elkanii

机译：一种酶两种构象状态记录:晶体结构的S-adenosyl-L-homocysteine水解酶从Bradyrhizobium elkanii

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摘要

S-Adenosyl-l-homocysteine hydrolase (SAHase) is involved in the enzymatic regulation of S-adenosyl-l-methionine (SAM)-dependent methylation reactions. After methyl-group transfer from SAM, S-adenosyl-l-homocysteine (SAH) is formed as a byproduct, which in turn is hydrolyzed to adenosine (Ado) and homocysteine (Hcy) by SAHase. The crystal structure of BeSAHase, an SAHase from Bradyrhizobium elkanii, which is a nitrogen-fixing bacterial symbiont of legume plants, was determined at 1.7 angstrom resolution, showing the domain organization (substrate-binding domain, NAD(+) cofactor-binding domain and dimerization domain) of the subunits. The protein crystallized in its biologically relevant tetrameric form, with three subunits in a closed conformation enforced by complex formation with the Ado product of the enzymatic reaction. The fourth subunit is ligand-free and has an open conformation. The BeSAHase structure therefore provides a unique snapshot of the domain movement of the enzyme induced by the binding of its natural ligands.
机译：S-Adenosyl-l-homocysteine水解酶(SAHase)参与酶的监管S-adenosyl-l-methionine (SAM)端依赖甲基化反应。从山姆,S-adenosyl-l-homocysteine(SAH)形成副产品,反过来腺苷酸(Ado)和同型半胱氨酸水解由SAHase (Hcy)。这是一个固氮细菌共生有机体的豆科植物,决心为1.7埃分辨率,显示域的组织(substrate-binding域,NAD (+)cofactor-binding域和二聚作用域)子单元。生物相关的四聚物的形式,有三个子单元在一个封闭的构象被执行复杂地层与Ado的产物酶促反应。ligand-free并已开放的构象。因此提供了一个独特的BeSAHase结构域运动的快照的酶天然配体诱导的绑定。

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