Sökning: onr:"swepub:oai:DiVA.org:uu-134901" >
Staphylococcus aure...
Staphylococcus aureus elongation factor G - structure and analysis of a target for fusidic acid
-
- Chen, Yang (författare)
- Uppsala universitet,Institutionen för cell- och molekylärbiologi
-
- Koripella, Ravi Kiran (författare)
- Uppsala universitet,Institutionen för cell- och molekylärbiologi
-
- Sanyal, Suparna (författare)
- Uppsala universitet,Institutionen för cell- och molekylärbiologi
-
visa fler...
-
- Selmer, Maria (författare)
- Uppsala universitet,Institutionen för cell- och molekylärbiologi
-
visa färre...
-
(creator_code:org_t)
- 2010-08-13
- 2010
- Engelska.
-
Ingår i: The FEBS Journal. - : Wiley. - 1742-464X .- 1742-4658. ; 277:18, s. 3789-3803
- Relaterad länk:
-
https://febs.onlinel...
-
visa fler...
-
https://urn.kb.se/re...
-
https://doi.org/10.1...
-
visa färre...
Abstract
Ämnesord
Stäng
- Fusidic acid (FA) is a bacteriostatic antibiotic that locks elongation factor G (EF-G) on the ribosome in a post-translocational state. It is used clinically against Gram-positive bacteria such as pathogenic strains of Staphylococcus aureus, but no structural information has been available for EF-G from these species. We have solved the apo crystal structure of EF-G from S. aureus to 1.9 A resolution. This structure shows a dramatically different overall conformation from previous structures of EF-G, although the individual domains are highly similar. Between the different structures of free or ribosome-bound EF-G, domains III-V move relative to domains I-II, resulting in a displacement of the tip of domain IV relative to domain G. In S. aureus EF-G, this displacement is about 25 A relative to structures of Thermus thermophilus EF-G in a direction perpendicular to that in previous observations. Part of the switch I region (residues 46-56) is ordered in a helix, and has a distinct conformation as compared with structures of EF-Tu in the GDP and GTP states. Also, the switch II region shows a new conformation, which, as in other structures of free EF-G, is incompatible with FA binding. We have analysed and discussed all known fusA-based fusidic acid resistance mutations in the light of the new structure of EF-G from S. aureus, and a recent structure of T. thermophilus EF-G in complex with the 70S ribosome with fusidic acid [Gao YG et al. (2009) Science326, 694-699]. The mutations can be classified as affecting FA binding, EF-G-ribosome interactions, EF-G conformation, and EF-G stability.
Ämnesord
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Nyckelord
- antibiotic resistance
- crystallography
- elongation factor G (EF-G)
- fusidic acid
- switch region
- Biology
- Biologi
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas