1f60: Difference between revisions

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[[Image:1f60.jpg|left|200px]]<br /><applet load="1f60" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1f60.jpg|left|200px]]<br /><applet load="1f60" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1f60, resolution 1.67Å" />

'''CRYSTAL STRUCTURE OF THE YEAST ELONGATION FACTOR COMPLEX EEF1A:EEF1BA'''<br />

==Overview==

The crystal structure of a complex between the protein biosynthesis, elongation factor eEF1A (formerly EF-1alpha) and the catalytic C terminus, of its exchange factor, eEF1Balpha (formerly EF-1beta), was determined to, 1.67 A resolution. One end of the nucleotide exchange factor is buried, between the switch 1 and 2 regions of eEF1A and destroys the binding site, for the Mg(2+) ion associated with the nucleotide. The second end of, eEF1Balpha interacts with domain 2 of eEF1A in the region hypothesized to, be involved in the binding of the CCA-aminoacyl end of the tRNA. The, competition between eEF1Balpha and aminoacylated tRNA may be a central, element in channeling the reactants in eukaryotic protein synthesis. The, recognition of eEF1A by eEF1Balpha is very different from that observed in, the prokaryotic EF-Tu:EF-Ts complex. Recognition of the switch 2 region in, nucleotide exchange is, however, common to the elongation factor complexes, and those of Ras:Sos and Arf1:Sec7.

The crystal structure of a complex between the protein biosynthesis elongation factor eEF1A (formerly EF-1alpha) and the catalytic C terminus of its exchange factor, eEF1Balpha (formerly EF-1beta), was determined to 1.67 A resolution. One end of the nucleotide exchange factor is buried between the switch 1 and 2 regions of eEF1A and destroys the binding site for the Mg(2+) ion associated with the nucleotide. The second end of eEF1Balpha interacts with domain 2 of eEF1A in the region hypothesized to be involved in the binding of the CCA-aminoacyl end of the tRNA. The competition between eEF1Balpha and aminoacylated tRNA may be a central element in channeling the reactants in eukaryotic protein synthesis. The recognition of eEF1A by eEF1Balpha is very different from that observed in the prokaryotic EF-Tu:EF-Ts complex. Recognition of the switch 2 region in nucleotide exchange is, however, common to the elongation factor complexes and those of Ras:Sos and Arf1:Sec7.

==About this Structure==

1F60 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1F60 OCA].

1F60 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F60 OCA].

==Reference==

Line 13:

[[Category: Protein complex]]

[[Category: Saccharomyces cerevisiae]]

[[Category: Andersen, G.R.]]

[[Category: Andersen, G R.]]

[[Category: Kinzy, T.G.]]

[[Category: Kinzy, T G.]]

[[Category: Nyborg, J.]]

[[Category: Pedersen, L.]]

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[[Category: protein-protein complex]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:16 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1f60.jpg|left|200px]]<br /><applet load="1f60" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1f60.jpg|left|200px]]<br /><applet load="1f60" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1f60, resolution 1.67&Aring;" />
 '''CRYSTAL STRUCTURE OF THE YEAST ELONGATION FACTOR COMPLEX EEF1A:EEF1BA'''<br />
 ==Overview==
-The crystal structure of a complex between the protein biosynthesis, elongation factor eEF1A (formerly EF-1alpha) and the catalytic C terminus, of its exchange factor, eEF1Balpha (formerly EF-1beta), was determined to, 1.67 A resolution. One end of the nucleotide exchange factor is buried, between the switch 1 and 2 regions of eEF1A and destroys the binding site, for the Mg(2+) ion associated with the nucleotide. The second end of, eEF1Balpha interacts with domain 2 of eEF1A in the region hypothesized to, be involved in the binding of the CCA-aminoacyl end of the tRNA. The, competition between eEF1Balpha and aminoacylated tRNA may be a central, element in channeling the reactants in eukaryotic protein synthesis. The, recognition of eEF1A by eEF1Balpha is very different from that observed in, the prokaryotic EF-Tu:EF-Ts complex. Recognition of the switch 2 region in, nucleotide exchange is, however, common to the elongation factor complexes, and those of Ras:Sos and Arf1:Sec7.
+The crystal structure of a complex between the protein biosynthesis elongation factor eEF1A (formerly EF-1alpha) and the catalytic C terminus of its exchange factor, eEF1Balpha (formerly EF-1beta), was determined to 1.67 A resolution. One end of the nucleotide exchange factor is buried between the switch 1 and 2 regions of eEF1A and destroys the binding site for the Mg(2+) ion associated with the nucleotide. The second end of eEF1Balpha interacts with domain 2 of eEF1A in the region hypothesized to be involved in the binding of the CCA-aminoacyl end of the tRNA. The competition between eEF1Balpha and aminoacylated tRNA may be a central element in channeling the reactants in eukaryotic protein synthesis. The recognition of eEF1A by eEF1Balpha is very different from that observed in the prokaryotic EF-Tu:EF-Ts complex. Recognition of the switch 2 region in nucleotide exchange is, however, common to the elongation factor complexes and those of Ras:Sos and Arf1:Sec7.
 ==About this Structure==
-F60 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F60 OCA].
+F60 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F60 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Protein complex]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Andersen, G.R.]]
+[[Category: Andersen, G R.]]
-[[Category: Kinzy, T.G.]]
+[[Category: Kinzy, T G.]]
 [[Category: Nyborg, J.]]
 [[Category: Pedersen, L.]]
@@ Line 20: / Line 20: @@
 [[Category: protein-protein complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:38:48 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:16 2008''