The structure of S. lividans acetoacetyl-CoA synthetase shows a novel interaction between the C-terminal extension and the N-terminal domain
The structure of S. lividans acetoacetyl-CoA synthetase shows a novel interaction between the C-terminal extension and the N-terminal domain
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DOI：
10.1002/prot.24738
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发表时间：
2015-03-01
影响因子：
2.9
通讯作者：
Gulick, Andrew M.
中科院分区：
文献类型：
--
作者：
Mitchell, Carter A.;Tucker, Alex C.;Gulick, Andrew M.
腺苷单磷酸形成酰基辅酶A合成酶催化两步反应，其中涉及酰基腺苷酸的初始形成，酰基腺苷酸在第二部分反应中反应，在酰基底物和辅酶A之间形成硫酯。这些酶利用结构域交替催化机制，大约 110 个残基的 C 端结构域旋转 140 度，为两个部分反应形成不同的催化构象。乙酰乙酰辅酶 A 合成酶 (AacS) 的结构展示了该 C 末端结构域的一个新颖方面。具体而言，与该家族的其他成员相比，几种乙酰乙酰辅酶A 合成酶和乙酰乙酰辅酶A 合成酶在 C 末端含有 30 个残基延伸。尽管此延伸的残基在先前结构中是无序的，但 AacS 结构表明此延伸的残基可能与 N 端结构域的关键催化残基相互作用。蛋白质 2015; 83：575-581。 (c) 2014 年 Wiley 期刊公司。
The adenosine monoposphate-forming acyl-CoA synthetase enzymes catalyze a two-step reaction that involves the initial formation of an acyl adenylate that reacts in a second partial reaction to form a thioester between the acyl substrate and CoA. These enzymes utilize a Domain Alternation catalytic mechanism, whereby a approximate to 110 residue C-terminal domain rotates by 140 degrees to form distinct catalytic conformations for the two partial reactions. The structure of an acetoacetyl-CoA synthetase (AacS) is presented that illustrates a novel aspect of this C-terminal domain. Specifically, several acetyl- and acetoacetyl-CoA synthetases contain a 30-residue extension on the C-terminus compared to other members of this family. Whereas residues from this extension are disordered in prior structures, the AacS structure shows that residues from this extension may interact with key catalytic residues from the N-terminal domain. Proteins 2015; 83:575-581. (c) 2014 Wiley Periodicals, Inc.