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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >The high-resolution structure of pig heart succinyl-CoA:3-oxoacid coenzyme A transferase.
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The high-resolution structure of pig heart succinyl-CoA:3-oxoacid coenzyme A transferase.

机译：猪的高分辨率结构的心琥珀酰辅酶:3-oxoacid辅酶A转移酶。

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摘要

The enzyme succinyl-CoA:3-oxoacid coenzyme A transferase (SCOT) participates in the metabolism of ketone bodies in extrahepatic tissues. It catalyses the transfer of coenzyme A (CoA) from succinyl-CoA to acetoacetate with a classical ping-pong mechanism. There is biochemical evidence that the enzyme undergoes conformational changes during the reaction, but no domain movements have been reported in the available crystal structures. Here, a structure of pig heart SCOT refined at 1.5 A resolution is presented, showing that one of the four enzyme subunits in the crystallographic asymmetric unit has a molecule of glycerol bound in the active site; the glycerol molecule is hydrogen bonded to the conserved catalytic glutamate residue and is likely to occupy the cosubstrate-binding site. The binding of glycerol is associated with a substantial relative movement (a 13 degrees rotation) of two previously undefined domains that close around the substrate-binding site. The binding orientation of one of the cosubstrates, acetoacetate, is suggested based on the glycerol binding and the possibility that this dynamic domain movement is of functional importance is discussed.
机译：这种酶琥珀酰辅酶:3-oxoacid辅酶A转移酶(苏格兰人)参与新陈代谢酮体在肝外组织。催化作用的转移辅酶A (CoA)琥珀酰辅酶与古典乙酰乙酸盐乒乓机制。证据表明,酶会发生构象变化的反应,但是没有域在可用的动作已报告晶体结构。心苏格兰人精致的决议是1.5提出,表明四种酶之一子晶体不对称单位在积极分子的甘油绑定网站;守恒的催化谷氨酸残基,可能占领cosubstrate-binding网站。甘油与相关联的绑定大量相对运动(13度旋转)的两个以前未定义的域紧密围绕着substrate-binding网站。绑定的方向辅被用物之一,乙酰乙酸盐,提出基于甘油绑定和动态的可能性域的运动功能的重要性进行了讨论。

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