1nhy
From Proteopedia
(New page: 200px<br /><applet load="1nhy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nhy, resolution 3.0Å" /> '''Crystal Structure of ...) |
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| - | [[Image:1nhy.jpg|left|200px]]<br /><applet load="1nhy" size=" | + | [[Image:1nhy.jpg|left|200px]]<br /><applet load="1nhy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nhy, resolution 3.0Å" /> | caption="1nhy, resolution 3.0Å" /> | ||
'''Crystal Structure of the GST-like Domain of Elongation Factor 1-gamma from Saccharomyces cerevisiae.'''<br /> | '''Crystal Structure of the GST-like Domain of Elongation Factor 1-gamma from Saccharomyces cerevisiae.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the N-terminal 219 residues (domain 1) of the | + | The crystal structure of the N-terminal 219 residues (domain 1) of the conserved eukaryotic translation elongation factor 1Bgamma (eEF1Bgamma), encoded by the TEF3 gene in Saccharomyces cerevisiae, has been determined at 3.0 A resolution by the single wavelength anomalous dispersion technique. The structure is overall very similar to the glutathione S-transferase proteins and contains a pocket with architecture highly homologous to what is observed in glutathione S-transferase enzymes. The TEF3-encoded form of eEF1Bgamma has no obvious catalytic residue. However, the second form of eEF1Bgamma encoded by the TEF4 gene contains serine 11, which may act catalytically. Based on the x-ray structure and gel filtration studies, we suggest that the yeast eEF1 complex is organized as an [eEF1A.eEF1Balpha.eEF1Bgamma]2 complex. A 23-residue sequence in the middle of eEF1Bgamma is essential for the stable dimerization of eEF1Bgamma and the quaternary structure of the eEF1 complex. |
==About this Structure== | ==About this Structure== | ||
| - | 1NHY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1NHY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NHY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Andersen, G | + | [[Category: Andersen, G R.]] |
| - | [[Category: Jeppesen, M | + | [[Category: Jeppesen, M G.]] |
| - | [[Category: Kinzy, T | + | [[Category: Kinzy, T G.]] |
[[Category: Nyborg, J.]] | [[Category: Nyborg, J.]] | ||
[[Category: Ortiz, P.]] | [[Category: Ortiz, P.]] | ||
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[[Category: protein synthesis]] | [[Category: protein synthesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:06:15 2008'' |
Revision as of 12:06, 21 February 2008
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Crystal Structure of the GST-like Domain of Elongation Factor 1-gamma from Saccharomyces cerevisiae.
Overview
The crystal structure of the N-terminal 219 residues (domain 1) of the conserved eukaryotic translation elongation factor 1Bgamma (eEF1Bgamma), encoded by the TEF3 gene in Saccharomyces cerevisiae, has been determined at 3.0 A resolution by the single wavelength anomalous dispersion technique. The structure is overall very similar to the glutathione S-transferase proteins and contains a pocket with architecture highly homologous to what is observed in glutathione S-transferase enzymes. The TEF3-encoded form of eEF1Bgamma has no obvious catalytic residue. However, the second form of eEF1Bgamma encoded by the TEF4 gene contains serine 11, which may act catalytically. Based on the x-ray structure and gel filtration studies, we suggest that the yeast eEF1 complex is organized as an [eEF1A.eEF1Balpha.eEF1Bgamma]2 complex. A 23-residue sequence in the middle of eEF1Bgamma is essential for the stable dimerization of eEF1Bgamma and the quaternary structure of the eEF1 complex.
About this Structure
1NHY is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.
Reference
The crystal structure of the glutathione S-transferase-like domain of elongation factor 1Bgamma from Saccharomyces cerevisiae., Jeppesen MG, Ortiz P, Shepard W, Kinzy TG, Nyborg J, Andersen GR, J Biol Chem. 2003 Nov 21;278(47):47190-8. Epub 2003 Sep 12. PMID:12972429
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