期刊
JOURNAL OF STRUCTURAL BIOLOGY
卷 162, 期 1, 页码 152-169出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2007.11.002
关键词
phenylalanine tRNA synthetase; antibacterial drug design; rational mutagenesis; protein engineering; crystal structure
In this article, we describe for the first time the high-resolution crystal structure of a phenylalanine tRNA synthetase from the pathogenic bacterium Staphylococcus haemolyticus. We demonstrate the subtle yet important structural differences between this enzyme and the previously described Thermus thermophilus ortholog. We also explain the structure-activity relationship of several recently reported inhibitors. The native enzyme crystals were of poor quality-they only diffracted X-rays to 3-5 angstrom resolution. Therefore, we have executed a rational surface mutagenesis strategy that has yielded crystals of this 2300-amino acid multidomain protein, diffracting to 2 angstrom or better. This methodology is discussed and contrasted with the more traditional domain truncation approach. (C) 2007 Elsevier Inc. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据