1elo
ELONGATION FACTOR G WITHOUT NUCLEOTIDE
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OverviewOverview
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.
About this StructureAbout this Structure
1ELO is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus., AEvarsson A, Brazhnikov E, Garber M, Zheltonosova J, Chirgadze Y, al-Karadaghi S, Svensson LA, Liljas A, EMBO J. 1994 Aug 15;13(16):3669-77. PMID:8070397
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