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首页> 美国卫生研究院文献>Protein Science : A Publication of the Protein Society >Racemic crystallography of synthetic protein enantiomers used to determine the X-ray structure of plectasin by direct methods
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Racemic crystallography of synthetic protein enantiomers used to determine the X-ray structure of plectasin by direct methods

机译：合成蛋白对映体的外消旋晶体学用于通过直接方法确定Plectasin的X射线结构

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摘要

We describe the use of racemic crystallography to determine the X-ray structure of the natural product plectasin, a potent antimicrobial protein recently isolated from fungus. The protein enantiomers l-plectasin and d-plectasin were prepared by total chemical synthesis; interestingly, l-plectasin showed the expected antimicrobial activity, while d-plectasin was devoid of such activity. The mirror image proteins were then used for racemic crystallization. Synchrotron X-ray diffraction data were collected to atomic resolution from a racemic plectasin crystal; the racemate crystallized in the achiral centrosymmetric space group with one l-plectasin molecule and one d-plectasin molecule forming the unit cell. Dimer-like intermolecular interactions between the protein enantiomers were observed, which may account for the observed extremely low solvent content (13%–15%) and more highly ordered nature of the racemic crystals. The structure of the plectasin molecule was well defined for all 40 amino acids and was generally similar to the previously determined NMR structure, suggesting minimal impact of the crystal packing on the plectasin conformation.
机译：我们描述了使用消旋晶体学来确定天然产物Plectasin的X射线结构，Plectasin是一种最近从真菌中分离出来的有效抗菌蛋白。通过全化学合成制备蛋白质对映体l-plectasin和d-plectasin。有趣的是，l-Plectasin显示出预期的抗菌活性，而D-Plectasin则没有这种活性。然后将镜像蛋白用于外消旋结晶。从外消旋Plectasin晶体收集同步加速器X射线衍射数据至原子分辨率；外消旋体在非手性中心对称空间群中结晶，形成一个L-Plectasin分子和一个D-Plectasin分子形成晶胞。观察到蛋白质对映体之间的二聚体状分子间相互作用，这可能解释了观察到的极低溶剂含量（13％–15％）和外消旋晶体的高度有序性。 Plectasin分子的结构对于所有40个氨基酸均定义良好，并且通常类似于先前确定的NMR结构，表明晶体堆积对Plectasin构象的影响最小。

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