1efm
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(New page: 200px<br /><applet load="1efm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1efm, resolution 2.7Å" /> '''STRUCTURE OF THE GDP ...)
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Revision as of 11:50, 20 November 2007
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STRUCTURE OF THE GDP DOMAIN OF EF-TU AND LOCATION OF THE AMINO ACIDS HOMOLOGOUS TO RAS ONCOGENE PROTEINS
Overview
A 2.7 angstrom resolution x-ray diffraction analysis of a trypsin-modified, form of the Escherichia coli elongation factor Tu reveals that the, GDP-binding domain has a structure similar to that of other, nucleotide-binding proteins. The GDP ligand is located at the, COOH-terminal end of the beta sheet and is linked to the protein via a, Mg2+ ion salt bridge. The location of the guanine ring is unusual; the, purine ring is located on the outer edge of the domain, not deep within a, hydrophobic pocket. The amino acids from Pro10 to Arg44 and from Gly59 to, Glu190 have been assigned to the electron density with computer graphic, techniques, and the resulting model is consistent with all known, biochemical data. An analysis of the structure reveals that four regions, of the amino acid sequence that are homologous with the family of ras, oncogene proteins, termed p21, are located in the vicinity of the, GDP-binding site, and most of the invariant amino acids shared by the, proteins interact directly with the GDP ligand.
About this Structure
1EFM is a Single protein structure of sequence from Escherichia coli with MG and GDP as ligands. Full crystallographic information is available from OCA.
Reference
Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins., Jurnak F, Science. 1985 Oct 4;230(4721):32-6. PMID:3898365
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