1f60

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1f60" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f60, resolution 1.67&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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;" />
caption="1f60, resolution 1.67&Aring;" />
'''CRYSTAL STRUCTURE OF THE YEAST ELONGATION FACTOR COMPLEX EEF1A:EEF1BA'''<br />
'''CRYSTAL STRUCTURE OF THE YEAST ELONGATION FACTOR COMPLEX EEF1A:EEF1BA'''<br />
==Overview==
==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==
==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==
==Reference==
Line 13: Line 13:
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
-
[[Category: Andersen, G.R.]]
+
[[Category: Andersen, G R.]]
-
[[Category: Kinzy, T.G.]]
+
[[Category: Kinzy, T G.]]
[[Category: Nyborg, J.]]
[[Category: Nyborg, J.]]
[[Category: Pedersen, L.]]
[[Category: Pedersen, L.]]
Line 20: Line 20:
[[Category: protein-protein complex]]
[[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''

Revision as of 10:35, 21 February 2008


1f60, resolution 1.67Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF THE YEAST ELONGATION FACTOR COMPLEX EEF1A:EEF1BA

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.

About this Structure

1F60 is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha., Andersen GR, Pedersen L, Valente L, Chatterjee I, Kinzy TG, Kjeldgaard M, Nyborg J, Mol Cell. 2000 Nov;6(5):1261-6. PMID:11106763

Page seeded by OCA on Thu Feb 21 12:35:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools