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PDBsum entry 1nhy
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The crystal structure of the glutathione s-Transferase-Like domain of elongation factor 1bgamma from saccharomyces cerevisiae.
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Authors
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M.G.Jeppesen,
P.Ortiz,
W.Shepard,
T.G.Kinzy,
J.Nyborg,
G.R.Andersen.
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Ref.
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J Biol Chem, 2003,
278,
47190-47198.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 5.
FIG. 5. The putative active site of eEF1B  Tef3p.
The side chains of key residues in and around the active site of
GST proteins are shown in ball and stick. See text for further
discussion.
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Figure 6.
FIG. 6. Surface representation of conservation as described
in Fig. 4 mapped on the eEF1B domain 1 monomer.
Residues less than 50% identical are colored red, and blue
indicates 100% identity. Residues with between 50 and 100%
identity are colored gray. A, eEF1B viewed from the dimer
interface in the same orientation as Fig. 3A. B, view from the
solvent-exposed face. The three 100% conserved residues Thr-151,
Arg-190, and Thr-194 form a patch on the solvent-exposed side of
the N terminus of eEF1B .
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2003,
278,
47190-47198)
copyright 2003.
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