title: Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site.
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.
authors.affiliation: Department of Molecular Biophysics, Centre for Chemistry and Chemical Engineering, Lund University, Lund, SE-221 00, Sweden.
authors.forename: M
authors.initials: M
authors.lastname: Laurberg
authors.forename: O
authors.initials: O
authors.lastname: Kristensen
authors.forename: K
authors.initials: K
authors.lastname: Martemyanov
authors.forename: A T
authors.initials: AT
authors.lastname: Gudkov
authors.forename: I
authors.initials: I
authors.lastname: Nagaev
authors.forename: D
authors.initials: D
authors.lastname: Hughes
authors.forename: A
authors.initials: A
authors.lastname: Liljas
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D019943:Amino Acid Substitution / Q000235:genetics*; D001665:Binding Sites; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D004352:Drug Resistance, Microbial; D005672:Fusidic Acid / Q000378:metabolism; D006153:Guanosine Diphosphate / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D020653:Peptide Elongation Factor G / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017354:Point Mutation / Q000235:genetics*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D016963:Thermus thermophilus / Q000737:chemistry* / Q000235:genetics
chemical_list: D020653:Peptide Elongation Factor G; D006153:Guanosine Diphosphate; D005672:Fusidic Acid