Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site
Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site
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DOI：
10.1006/jmbi.2000.4168
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发表时间：
2000-11-03
影响因子：
5.6
通讯作者：
Liljas, A
中科院分区：
文献类型：
--
作者：
Laurberg, M;Kristensen, O;Liljas, A
以2.8埃的分辨率测定了携带点突变His 573 Ala的嗜热栖热菌延伸因子G（EF-G）的晶体结构。该突变体具有比先前报道的野生型EF-G更封闭的结构。这是通过域III、IV和V相对于域I和II的10度刚性旋转获得的。这种旋转导致畴TV的尖端位移约9埃。结构域III的结构现在完全可见，并揭示了EFG结构域V和几种核糖体蛋白也观察到的双分裂β-α-β基序。在结构域III中发现的大量夫西地酸抗性突变现在已经可以定位。关于一些夫西地酸耐药突变的效应环和夫西地酸的可能的结合位点的可能的位置进行了讨论。(C)北京大学出版社.
The crystal structure of Thermus thermophilus elongation factor G (EF-G) carrying the point mutation His573Ala was determined at a resolution of 2.8 Angstrom. The mutant has a more closed structure than that previously reported for wild-type EF-G. This is obtained by a 10 degrees rigid rotation of domains III, TV and V with regard to domains I and II. This rotation results in a displacement of the tip of domain TV by approximately 9 Angstrom. The structure of domain III is now fully visible and reveals the double split beta-alpha-beta motif also observed for EFG domain V and for several ribosomal proteins. A large number of fusidic acid resistant mutations found in domain III have now been possible to locate. Possible locations for the effector loop and a possible binding site for fusidic acid are discussed in relation to some of the fusidic acid resistant mutations. (C) 2000 Academic Press.