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酪氨酰-tRNA合成酶：人类线粒体氨酰-tRNA合成酶的首次结晶。

Tyrosyl-tRNA synthetase: the first crystallization of a human mitochondrial aminoacyl-tRNA synthetase.

作者信息

Bonnefond Luc, Frugier Magali, Touzé Elodie, Lorber Bernard, Florentz Catherine, Giegé Richard, Rudinger-Thirion Joëlle, Sauter Claude

机构信息

Département Machineries Traductionnelles, Architecture et Réactivité de l'ARN, Université Louis Pasteur de Strasbourg, CNRS, IBMC, Strasbourg, France.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Apr 1;63(Pt 4):338-41. doi: 10.1107/S1744309107012481. Epub 2007 Mar 30.

DOI:10.1107/S1744309107012481
PMID:17401211
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2330213/
Abstract

Human mitochondrial tyrosyl-tRNA synthetase and a truncated version with its C-terminal S4-like domain deleted were purified and crystallized. Only the truncated version, which is active in tyrosine activation and Escherichia coli tRNA(Tyr) charging, yielded crystals suitable for structure determination. These tetragonal crystals, belonging to space group P4(3)2(1)2, were obtained in the presence of PEG 4000 as a crystallizing agent and diffracted X-rays to 2.7 A resolution. Complete data sets could be collected and led to structure solution by molecular replacement.

摘要

人类线粒体酪氨酸-tRNA合成酶及其C末端S4样结构域缺失的截短版本被纯化并结晶。只有截短版本在酪氨酸激活和大肠杆菌tRNA（Tyr）充电中具有活性，产生了适合结构测定的晶体。这些四方晶体属于空间群P4(3)2(1)2，在作为结晶剂的聚乙二醇4000存在下获得，并将X射线衍射到2.7埃分辨率。可以收集完整的数据集，并通过分子置换进行结构解析。

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