Structure of PatF from Prochloron didemni.
Structure of PatF from Prochloron didemni.
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DOI：
10.1107/s1744309113012931
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发表时间：
2013-06
期刊：
影响因子：
--
通讯作者：
Naismith JH
中科院分区：
文献类型：
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作者：
Bent AF;Koehnke J;Houssen WE;Smith MC;Jaspars M;Naismith JH
用单波长反常衍射法对白纹伊蚊PATF的X-射线晶体结构进行了解析，其分辨率为2.13 á。Patellamide是具有强大生物效应的大环肽，是氰基结合蛋白的一个子集。氰基结合蛋白是由一系列的酶转化而成的天然产物，一种常见的修饰是加成一个戊烯基团。令人费解的是，白鲜杆菌中的帕特拉胺途径包含一个与戊烯基酶同源的基因patF，但帕特莱胺本身并不是丙烯化的。克隆、表达、纯化和鉴定了PatF蛋白的结构。不能证明该蛋白质的丙氨酸酶活性，结构检查显示活性部位的侧链同一性发生了变化。据推测，这些变化已经使该蛋白质失活。突变这些残基的尝试导致了蛋白质的未折叠。
The X-ray crystal structure of PatF from P. didemni was solved by the single-wavelength anomalous diffraction method to a resolution of 2.13 Å. Patellamides are macrocyclic peptides with potent biological effects and are a subset of the cyanobactins. Cyanobactins are natural products that are produced by a series of enzymatic transformations and a common modification is the addition of a prenyl group. Puzzlingly, the pathway for patellamides in Prochloron didemni contains a gene, patF, with homology to prenylases, but patellamides are not themselves prenylated. The structure of the protein PatF was cloned, expressed, purified and determined. Prenylase activity could not be demonstrated for the protein, and examination of the structure revealed changes in side-chain identity at the active site. It is suggested that these changes have inactivated the protein. Attempts to mutate these residues led to unfolded protein.