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J Mol Biol. 2000 Nov 3;303(4):593-603.

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

Author information

1
Department of Molecular Biophysics, Centre for Chemistry and Chemical Engineering, Lund University, Lund, SE-221 00, Sweden.

Abstract

The crystal structure of Thermus thermophilus elongation factor G (EF-G) carrying the point mutation His573Ala was determined at a resolution of 2.8 A. 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, 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 A. The structure of domain III is now fully visible and reveals the double split beta-alpha-beta 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.

PMID:
11054294
DOI:
10.1006/jmbi.2000.4168
[Indexed for MEDLINE]

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