Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site
Research output: Contribution to journal › Journal article › Research › peer-review
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.
Original language | English |
---|---|
Journal | Journal of Molecular Biology |
Volume | 303 |
Issue number | 4 |
Pages (from-to) | 593-603 |
Number of pages | 11 |
ISSN | 0022-2836 |
DOIs | |
Publication status | Published - 2000 |
Externally published | Yes |
- Amino Acid Motifs, Amino Acid Sequence, Amino Acid Substitution, Binding Sites, Conserved Sequence, Crystallography, X-Ray, Drug Resistance, Microbial, Fusidic Acid, Guanosine Diphosphate, Models, Molecular, Molecular Sequence Data, Peptide Elongation Factor G, Point Mutation, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Alignment, Thermus thermophilus
Research areas
ID: 47416685