Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site

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• 作者：Laurberg ; Martin ; Kristensen ; Ole ; Martemyanov ; Kirill ; Gudkov ; Anatoly T. ; Nagaev ; Ivan ; Hughes ; Diarmaid ; et. al.
• 关键词：proteins synthesis ; elongation factor G ; crystal structure ; conformational change ; fusidic acid resistance ; EF-G ; elongation factor G ; GDP ; guanosine 5&prime ; -diphosphate ; GTP ; guanosine 5&prime ; -triphosphate ; GDPNP ; guanylyl imidodiphosphate ; GDPCP ; phos
• 刊名：Journal of Molecular Biology
• 出版年：2000
• 出版时间：November 3, 2000
• 年：2000
• 卷：303
• 期：4
• 页码：593-603
• 全文大小：377 K

文摘

The crystal structure of Thermus thermophilus elongation factor G (EF-G) carrying the point mutation His573Ala was determined at a resolution of 2.8 Å. The mutant has a more closed structure than that previously reported for wild-type EF-G. This is obtained by a 10° rigid rotation of domains III, IV and V with regard to domains I and II. This rotation results in a displacement of the tip of domain IV by approximately 9 Å. The structure of domain III is now fully visible and reveals the double split β-α-β motif also observed for EF-G 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.