1FNM

STRUCTURE OF THERMUS THERMOPHILUS EF-G H573A

Summary for 1FNM

• Entry DOI: 10.2210/pdb1fnm/pdb
• Descriptor: ELONGATION FACTOR G, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: bent conformation, visible domain iii, mutation his573ala, translation
• Biological source: Thermus thermophilus
• Cellular location: Cytoplasm: P13551
• Total number of polymer chains: 1
• Total formula weight: 77377.54

Authors

Laurberg, M.,Kristensen, O.,Martemyanov, K.,Gudkov, A.T.,Nagaev, I.,Hughes, D.,Liljas, A. (deposition date: 2000-08-22, release date: 2000-11-22, Last modification date: 2024-02-07)

Primary citation

Laurberg, M.,Kristensen, O.,Martemyanov, K.,Gudkov, A.T.,Nagaev, I.,Hughes, D.,Liljas, A.
Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site.
J.Mol.Biol., 303:593-603, 2000

PubMed Abstract: 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.

PubMed: 11054294
DOI: 10.1006/jmbi.2000.4168

Experimental method

X-RAY DIFFRACTION (2.8 Å)