Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site
2000 (English)In: Journal of Molecular Biology, ISSN 0022-2836, E-ISSN 1089-8638, Vol. 303, no 4, 593-603 p.Article in journal (Refereed) Published
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 previouslyreported for wild-type EF-G. This is obtained by a 10° rigid rotation of domains III, IV and V with regardto domains I and II. This rotation results in a displacement of the tipof domain IV by approximately 9 Å. The structure of domain III is nowfully 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 tolocate. Possible locations for the effector loop and a possible bindingsite for fusidic acid are discussed in relation to some of the fusidic acid resistant mutations.
Place, publisher, year, edition, pages
2000. Vol. 303, no 4, 593-603 p.
Microbiology in the medical area
IdentifiersURN: urn:nbn:se:uu:diva-44850DOI: 10.1006/jmbi.2000.4168OAI: oai:DiVA.org:uu-44850DiVA: diva2:72756