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TitleThree-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus.
Journal, issue, pagesEMBO J, Vol. 13, Issue 16, Page 3669-3677, Year 1994
Publish dateAug 15, 1994
AuthorsA AEvarsson / E Brazhnikov / M Garber / J Zheltonosova / Y Chirgadze / S al-Karadaghi / L A Svensson / A Liljas /
PubMed AbstractThe 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 linksEMBO J / PubMed:8070397 / PubMed Central
MethodsX-ray diffraction
Resolution2.8 Å
Structure data

PDB-1elo:
ELONGATION FACTOR G WITHOUT NUCLEOTIDE
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Source
  • thermus thermophilus (bacteria)
KeywordsELONGATION FACTOR / RIBOSOMAL TRANSLOCASE / GTP BINDING PROTEIN / HYDROLASE

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