Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus.
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.
AEvarsson
A
A
Department of Molecular Biophysics, University of Lund, Sweden.
Brazhnikov
E
E
Garber
M
M
Zheltonosova
J
J
Chirgadze
Y
Y
al-Karadaghi
S
S
Svensson
L A
LA
Liljas
A
A
D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D020963:GTP Phosphohydrolase-Linked Elongation Factors / Q000737:chemistry* / Q000378:metabolism; D006153:Guanosine Diphosphate / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D016601:RNA-Binding Proteins / Q000737:chemistry; D012269:Ribosomal Proteins / Q000737:chemistry; D016963:Thermus thermophilus / Q000737:chemistry / Q000201:enzymology*
D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors; D016601:RNA-Binding Proteins; D012269:Ribosomal Proteins; D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate; D020963:GTP Phosphohydrolase-Linked Elongation Factors