来自假单胞菌属菌株AAC的丙二酸半醛脱氢酶的X射线晶体结构。
X-ray crystal structure of a malonate-semialdehyde dehydrogenase from Pseudomonas sp. strain AAC.
作者信息
Wilding Matthew, Scott Colin, Peat Thomas S, Newman Janet
机构信息
Land and Water, CSIRO, GPO Box 1700, Canberra, ACT 2601, Australia.
Biomedical Program, Manufacturing, CSIRO, 343 Royal Parade, Parkville, VIC 3052, Australia.
出版信息
Acta Crystallogr F Struct Biol Commun. 2017 Jan 1;73(Pt 1):24-28. doi: 10.1107/S2053230X16020008.
Abstract
The NAD-dependent malonate-semialdehyde dehydrogenase KES23460 from Pseudomonas sp. strain AAC makes up half of a bicistronic operon responsible for β-alanine catabolism to produce acetyl-CoA. The KES23460 protein has been heterologously expressed, purified and used to generate crystals suitable for X-ray diffraction studies. The crystals belonged to space group P222 and diffracted X-rays to beyond 3 Å resolution using the microfocus beamline of the Australian Synchrotron. The structure was solved using molecular replacement, with a monomer from PDB entry 4zz7 as the search model.
摘要
来自假单胞菌属菌株AAC的NAD依赖型丙二酸半醛脱氢酶KES23460构成了一个双顺反子操纵子的一半，该操纵子负责β-丙氨酸分解代谢以产生乙酰辅酶A。KES23460蛋白已被异源表达、纯化，并用于生成适合X射线衍射研究的晶体。这些晶体属于空间群P222，使用澳大利亚同步加速器的微聚焦光束线，其X射线衍射分辨率超过3 Å。该结构通过分子置换法解析，使用PDB条目4zz7中的一个单体作为搜索模型。
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