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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Crystallography, X-Ray
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GTP Phosphohydrolase-Linked Elongation Factors / chemistry*
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GTP Phosphohydrolase-Linked Elongation Factors / metabolism
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Guanosine Diphosphate / metabolism
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Guanosine Triphosphate / metabolism
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Models, Biological
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Models, Molecular
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Molecular Sequence Data
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Peptide Elongation Factor G
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Peptide Elongation Factors / chemistry*
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Peptide Elongation Factors / metabolism
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Protein Conformation
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RNA-Binding Proteins / chemistry
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Ribosomal Proteins / chemistry
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Thermus thermophilus / chemistry
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Thermus thermophilus / enzymology*
Substances
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Peptide Elongation Factor G
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Peptide Elongation Factors
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RNA-Binding Proteins
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Ribosomal Proteins
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Guanosine Diphosphate
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Guanosine Triphosphate
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GTP Phosphohydrolase-Linked Elongation Factors