来自假单胞菌属菌株AAC的腐胺转氨酶的晶体结构
Crystal structure of a putrescine aminotransferase from Pseudomonas sp. strain AAC.
作者信息
Wilding Matthew, Scott Colin, Newman Janet, Peat Thomas S
机构信息
Land and Water, CSIRO, GPO Box 1700, Canberra, ACT 2601, Australia.
Biomedical Program, CSIRO, 343 Royal Parade, Parkville, VIC 3052, Australia.
出版信息
Acta Crystallogr F Struct Biol Commun. 2017 Jan 1;73(Pt 1):29-35. doi: 10.1107/S2053230X16019658.
Abstract
The putrescine aminotransferase KES24511 from Pseudomonas sp. strain AAC was previously identified as an industrially relevant enzyme based on the discovery that it is able to promiscuously catalyse the transamination of 12-aminododecanoic acid. Here, the cloning, heterologous expression, purification and successful crystallization of the KES24511 protein are reported, which ultimately generated crystals adopting space group I2. The crystals diffracted X-rays to 2.07 Å resolution and data were collected using the microfocus beamline of the Australian Synchrotron. The structure was solved using molecular replacement, with a monomer from PDB entry 4a6t as the search model.
摘要
来自假单胞菌属菌株AAC的腐胺转氨酶KES24511先前已被鉴定为一种具有工业相关性的酶，这是基于发现它能够无差别地催化12-氨基十二烷酸的转氨作用。在此，报告了KES24511蛋白的克隆、异源表达、纯化和成功结晶，最终得到了属于空间群I2的晶体。这些晶体的X射线衍射分辨率达到2.07 Å，并使用澳大利亚同步加速器的微聚焦光束线收集了数据。该结构通过分子置换法解析，以PDB条目4a6t中的一个单体作为搜索模型。
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