三钛酰基-CoA 抑制琥珀酰-CoA 合成酶。
Tartryl-CoA inhibits succinyl-CoA synthetase.
机构信息
Department of Biological Sciences, University of Calgary, 2500 University Drive NW, Calgary, Alberta T2N 1N4, Canada.
出版信息
Acta Crystallogr F Struct Biol Commun. 2020 Jul 1;76(Pt 7):302-308. doi: 10.1107/S2053230X20008201.
Abstract
Succinyl-CoA synthetase (SCS) catalyzes the only substrate-level phosphorylation step in the tricarboxylic acid cycle. Human GTP-specific SCS (GTPSCS), an αβ-heterodimer, was produced in Escherichia coli. The purified protein crystallized from a solution containing tartrate, CoA and magnesium chloride, and a crystal diffracted to 1.52 Å resolution. Tartryl-CoA was discovered to be bound to GTPSCS. The CoA portion lies in the amino-terminal domain of the α-subunit and the tartryl end extends towards the catalytic histidine residue. The terminal carboxylate binds to the phosphate-binding site of GTPSCS.
摘要
琥珀酰辅酶 A 合成酶 (SCS) 催化三羧酸循环中唯一的底物水平磷酸化步骤。人 GTP 特异性 SCS (GTPSCS) 是一种 αβ 异二聚体，在大肠杆菌中产生。从含有酒石酸盐、辅酶 A 和氯化镁的溶液中纯化的蛋白质结晶，晶体衍射分辨率为 1.52 Å。发现酒石酰辅酶 A 与 GTPSCS 结合。辅酶 A 部分位于 α 亚基的氨基末端结构域，酒石酰末端朝向催化组氨酸残基。末端羧酸盐结合到 GTPSCS 的磷酸结合位点。
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