1ELO

ELONGATION FACTOR G WITHOUT NUCLEOTIDE

Summary for 1ELO

• Entry DOI: 10.2210/pdb1elo/pdb
• Descriptor: ELONGATION FACTOR G (1 entity in total)
• Functional Keywords: ribosomal translocase, gtp binding protein, hydrolase, elongation factor
• Biological source: Thermus thermophilus
• Cellular location: Cytoplasm: Q5SHN5
• Total number of polymer chains: 1
• Total formula weight: 76977.10

Authors

Aevarsson, A.,Brazhnikov, E.,Garber, M.,Zheltonosova, J.,Chirgadze, Yu.,Al-Karadaghi, S.,Svensson, L.A.,Liljas, A. (deposition date: 1996-03-13, release date: 1996-08-01, Last modification date: 2024-02-07)

Primary citation

AEvarsson, A.,Brazhnikov, E.,Garber, M.,Zheltonosova, J.,Chirgadze, Y.,al-Karadaghi, S.,Svensson, L.A.,Liljas, A.
Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus.
EMBO J., 13:3669-3677, 1994

PubMed Abstract: The crystal structure of Thermus thermophilus elongation factor G without guanine nucleotide was determined to 2.85 A. This GTPase has five domains with overall dimensions of 50 x 60 x 118 A. The GTP binding domain has a core common to other GTPases with a unique subdomain which probably functions as an intrinsic nucleotide exchange factor. Domains I and II are homologous to elongation factor Tu and their arrangement, both with and without GDP, is more similar to elongation factor Tu in complex with a GTP analogue than with GDP. Domains III and V show structural similarities to ribosomal proteins. Domain IV protrudes from the main body of the protein and has an extraordinary topology with a left-handed cross-over connection between two parallel beta-strands.

PubMed: 8070397

Experimental method

X-RAY DIFFRACTION (2.8 Å)