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. 1994 Aug 15;13(16):3669–3677. doi: 10.1002/j.1460-2075.1994.tb06676.x

Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus.

A AEvarsson 1, E Brazhnikov 1, M Garber 1, J Zheltonosova 1, Y Chirgadze 1, S al-Karadaghi 1, L A Svensson 1, A Liljas 1
PMCID: PMC395277  PMID: 8070397

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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