期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 66, 期 -, 页码 1326-1334出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309110037619
关键词
-
资金
- NIH, National Institute of General Medical Sciences, Protein Structure Initiative [U54 GM074898]
- DOE, OBER
- NIH (NCRR, BTP and NIGMS)
- US Department of Energy at Lawrence Berkeley National Laboratory [DE-AC02-05CH11231]
- National Institutes of Health, National Institute of General Medical Sciences
A novel aminoacyl-tRNA synthetase that contains an iron-sulfur cluster in the tRNA anticodon-binding region and efficiently charges tRNA with tryptophan has been found in Thermotoga maritima. The crystal structure of TmTrpRS (tryptophanyl-tRNA synthetase; TrpRS; EC 6.1.1.2) reveals an iron-sulfur [4Fe-4S] cluster bound to the tRNA anticodon-binding (TAB) domain and an l-tryptophan ligand in the active site. None of the other T. maritima aminoacyl-tRNA synthetases (AARSs) contain this [4Fe-4S] cluster-binding motif (C-x(22)-C-x(6)-C-x(2)-C). It is speculated that the iron-sulfur cluster contributes to the stability of TmTrpRS and could play a role in the recognition of the anticodon.
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