1fnm

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1fnm, resolution 2.80Å ()
Ligands: ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

STRUCTURE OF THERMUS THERMOPHILUS EF-G H573A

Publication Abstract from PubMed

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.

Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site., Laurberg M, Kristensen O, Martemyanov K, Gudkov AT, Nagaev I, Hughes D, Liljas A, J Mol Biol. 2000 Nov 3;303(4):593-603. PMID:11054294

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1fnm is a 1 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

See Also

Reference

  • Laurberg M, Kristensen O, Martemyanov K, Gudkov AT, 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. 2000 Nov 3;303(4):593-603. PMID:11054294 doi:10.1006/jmbi.2000.4168

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