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Title
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Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus.
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Authors
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A.AEvarsson,
E.Brazhnikov,
M.Garber,
J.Zheltonosova,
Y.Chirgadze,
S.al-Karadaghi,
L.A.Svensson,
A.Liljas.
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Ref.
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Embo J, 1994,
13,
3669-3677.
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PubMed id
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Abstract
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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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