1efm: Difference between revisions

Revision as of 13:27, 21 February 2008

STRUCTURE OF THE GDP DOMAIN OF EF-TU AND LOCATION OF THE AMINO ACIDS HOMOLOGOUS TO RAS ONCOGENE PROTEINS

OverviewOverview

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 StructureAbout this Structure

1EFM is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 12:27:11 2008

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OCA

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-[[Image:1efm.jpg|left|200px]]<br /><applet load="1efm" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1efm, resolution 2.7&Aring;" />
 '''STRUCTURE OF THE GDP DOMAIN OF EF-TU AND LOCATION OF THE AMINO ACIDS HOMOLOGOUS TO RAS ONCOGENE PROTEINS'''<br />
 ==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.
+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==
-EFM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG and GDP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EFM OCA].
+EFM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EFM OCA].
 ==Reference==
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 [[Category: elongation factor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:57:55 2007''
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