+Search query
-Structure paper
Title | Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus. |
---|---|
Journal, issue, pages | EMBO J, Vol. 13, Issue 16, Page 3669-3677, Year 1994 |
Publish date | Aug 15, 1994 |
Authors | A AEvarsson / E Brazhnikov / M Garber / J Zheltonosova / Y Chirgadze / S al-Karadaghi / L A Svensson / A Liljas / |
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 ...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. |
External links | EMBO J / PubMed:8070397 / PubMed Central |
Methods | X-ray diffraction |
Resolution | 2.8 Å |
Structure data | PDB-1elo: |
Source |
|
Keywords | ELONGATION FACTOR / RIBOSOMAL TRANSLOCASE / GTP BINDING PROTEIN / HYDROLASE |