1nhy
From Proteopedia
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|PDB= 1nhy |SIZE=350|CAPTION= <scene name='initialview01'>1nhy</scene>, resolution 3.0Å | |PDB= 1nhy |SIZE=350|CAPTION= <scene name='initialview01'>1nhy</scene>, resolution 3.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= TEF3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= TEF3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[3ljr|3LJR]], [[1fw1|1FW1]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nhy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nhy OCA], [http://www.ebi.ac.uk/pdbsum/1nhy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nhy RCSB]</span> | ||
}} | }} | ||
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[[Category: Nyborg, J.]] | [[Category: Nyborg, J.]] | ||
[[Category: Ortiz, P.]] | [[Category: Ortiz, P.]] | ||
| - | [[Category: SO4]] | ||
[[Category: gst-like]] | [[Category: gst-like]] | ||
[[Category: protein synthesis]] | [[Category: protein synthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:30:40 2008'' |
Revision as of 19:30, 30 March 2008
| |||||||
| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | TEF3 (Saccharomyces cerevisiae) | ||||||
| Related: | 3LJR, 1FW1
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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