PDBsum entry 1nhy

Translation

PDB id: 1nhy

Contents

Protein chain

219 a.a. *

Ligands

SO4

* Residue conservation analysis

PDB id:

1nhy

Name:

Translation

Title:

Crystal structure of the gst-like domain of elongation factor 1-gamma from saccharomyces cerevisiae.

Structure:

Elongation factor 1-gamma 1. Chain: a. Fragment: residue 1-219, n-terminal domain. Synonym: ef-1-gamma 1. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: tef3. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

Biol. unit:

Dimer (from PQS)

Resolution:

3.00Å R-factor: 0.235 R-free: 0.235

Authors:

M.G.Jeppesen,P.Ortiz,T.G.Kinzy,G.R.Andersen,J.Nyborg

Key ref:

M.G.Jeppesen et al. (2003). The crystal structure of the glutathione S-transferase-like domain of elongation factor 1Bgamma from Saccharomyces cerevisiae. J Biol Chem, 278, 47190-47198. PubMed id: 12972429 DOI: 10.1074/jbc.M306630200

Date:

20-Dec-02 Release date: 14-Jan-03

Protein chain

P29547  (EF1G1_YEAST) -  Elongation factor 1-gamma 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 415 a.a.

Struc: 219 a.a.

DOI no: 10.1074/jbc.M306630200

J Biol Chem 278:47190-47198 (2003)

PubMed id: 12972429

The crystal structure of the glutathione S-transferase-like domain of elongation factor 1Bgamma from Saccharomyces cerevisiae.

M.G.Jeppesen, P.Ortiz, W.Shepard, T.G.Kinzy, J.Nyborg, G.R.Andersen.

ABSTRACT

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.

Selected figure(s)

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.

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 .

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2003, 278, 47190-47198) copyright 2003.

Figures were selected by an automated process.