1f60: Difference between revisions

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[[Image:1f60.~~jpg~~|left|200px]]

[[Image:1f60.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF THE YEAST ELONGATION FACTOR COMPLEX EEF1A:EEF1BA~~'''~~

===CRYSTAL STRUCTURE OF THE YEAST ELONGATION FACTOR COMPLEX EEF1A:EEF1BA===

~~==Overview==~~

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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 line below this paragraph, {{ABSTRACT_PUBMED_11106763}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11106763 is the PubMed ID number.

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==About this Structure==

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[[Category: Valente, L.]]

[[Category: Protein-protein complex]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 15~~:56:46 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:45:22 2008''

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-[[Image:1f60.jpg|left|200px]]
+{{Seed}}
+[[Image:1f60.png|left|200px]]
 <!--
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 {{STRUCTURE_1f60|  PDB=1f60  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE YEAST ELONGATION FACTOR COMPLEX EEF1A:EEF1BA'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11106763}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11106763 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11106763}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Valente, L.]]
 [[Category: Protein-protein complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:56:46 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 02:45:22 2008''