uu.seUppsala University Publications
Change search
ReferencesLink to record
Permanent link

Direct link
Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site
Show others and affiliations
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
Abstract [en]

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.
National Category
Microbiology in the medical area
URN: urn:nbn:se:uu:diva-44850DOI: 10.1006/jmbi.2000.4168OAI: oai:DiVA.org:uu-44850DiVA: diva2:72756
Available from: 2008-05-27 Created: 2008-05-27 Last updated: 2011-07-18Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full text

Search in DiVA

By author/editor
Hughes, Diarmaid
By organisation
Department of Cell and Molecular Biology
In the same journal
Journal of Molecular Biology
Microbiology in the medical area

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 230 hits
ReferencesLink to record
Permanent link

Direct link