1nhy: Difference between revisions

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Crystal Structure of the GST-like Domain of Elongation Factor 1-gamma from Saccharomyces cerevisiae.

OverviewOverview

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 StructureAbout this Structure

1NHY is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 14:06:15 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1nhy.jpg|left|200px]]<br /><applet load="1nhy" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1nhy.jpg|left|200px]]<br /><applet load="1nhy" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1nhy, resolution 3.0&Aring;" />
 '''Crystal Structure of the GST-like Domain of Elongation Factor 1-gamma from Saccharomyces cerevisiae.'''<br />
 ==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.
+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==
-NHY 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NHY OCA].
+NHY 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==
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 [[Category: Saccharomyces cerevisiae]]
 [[Category: Single protein]]
-[[Category: Andersen, G.R.]]
+[[Category: Andersen, G R.]]
-[[Category: Jeppesen, M.G.]]
+[[Category: Jeppesen, M G.]]
-[[Category: Kinzy, T.G.]]
+[[Category: Kinzy, T G.]]
 [[Category: Nyborg, J.]]
 [[Category: Ortiz, P.]]
@@ Line 22: / Line 22: @@
 [[Category: protein synthesis]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:16:29 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:06:15 2008''