2XEX

crystal structure of Staphylococcus aureus elongation factor G

Summary for 2XEX

• Entry DOI: 10.2210/pdb2xex/pdb
• Descriptor: ELONGATION FACTOR G, POTASSIUM ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: gtpase, translation, biosynthetic protein
• Biological source: STAPHYLOCOCCUS AUREUS
• Cellular location: Cytoplasm: P68790
• Total number of polymer chains: 2
• Total formula weight: 153547.68

Authors

Chen, Y.,Koripella, R.K.,Sanyal, S.,Selmer, M. (deposition date: 2010-05-19, release date: 2010-07-14, Last modification date: 2023-12-20)

Primary citation

Chen, Y.,Koripella, R.K.,Sanyal, S.,Selmer, M.
Staphylococcus Aureus Elongation Factor G - Structure and Analysis of a Target for Fusidic Acid.
FEBS J., 277:3789-, 2010

PubMed Abstract: 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 Å 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 Å 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.

PubMed: 20718859
DOI: 10.1111/J.1742-4658.2010.07780.X

Experimental method

X-RAY DIFFRACTION (1.9 Å)