Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus. |
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| Authors: | A AEvarsson E Brazhnikov M Garber J Zheltonosova Y Chirgadze S al-Karadaghi L A Svensson A Liljas |
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| Affiliation: | Department of Molecular Biophysics, University of Lund, Sweden. |
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| 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. |
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