PDBsum entry 2fx3

Translation

PDB id: 2fx3

Contents

Protein chain

387 a.a. *

Ligands

GDP

Metals

_MG

Waters ×4

* Residue conservation analysis

PDB id:

2fx3

Name:

Translation

Title:

Crystal structure determination of e. Coli elongation factor, tu using a twinned data set

Structure:

Elongation factor tu. Chain: a. Synonym: ef-tu

Source:

Escherichia coli. Organism_taxid: 562. Other_details: gene: tufa

Biol. unit:

Dimer (from PQS)

Resolution:

3.40Å R-factor: 0.197 R-free: 0.262

Authors:

S.E.Heffron,R.Moeller,F.Jurnak

Key ref:

S.E.Heffron et al. (2006). Solving the structure of Escherichia coli elongation factor Tu using a twinned data set. Acta Crystallogr D Biol Crystallogr, 62, 433-438. PubMed id: 16552145 DOI: 10.1107/S0907444906004021

Date:

03-Feb-06 Release date: 28-Mar-06

Protein chain

P0CE47  (EFTU1_ECOLI) -  Elongation factor Tu 1 from Escherichia coli (strain K12)

Seq: 394 a.a.

Struc: 387 a.a.

DOI no: 10.1107/S0907444906004021

Acta Crystallogr D Biol Crystallogr 62:433-438 (2006)

PubMed id: 16552145

Solving the structure of Escherichia coli elongation factor Tu using a twinned data set.

S.E.Heffron, R.Moeller, F.Jurnak.

ABSTRACT

Escherichia coli elongation factor Tu-GDP (EF-Tu-GDP) was crystallized in the presence of novel inhibitors. The only crystals which could be grown were epitaxially as well as merohedrally twinned, highly mosaic and diffracted to a resolution of 3.4 A in space group P3(1)21, with unit-cell parameters a = b = 69.55, c = 169.44 A, alpha = beta = 90, gamma = 120 degrees . To determine whether an inhibitor was present in the crystal, a poor-quality X-ray diffraction data set had to be processed. The three-dimensional structure was ultimately solved and the original question answered. The results also reveal a new type of dimer packing for EF-Tu-GDP.

Selected figure(s)

Figure 3.
Figure 3 Stereo images of EF-Tu-MgGDP dimer interactions in the P3[1]21 crystals. One molecule of the EF-Tu dimer is shown as a blue ribbon and the symmetry-related molecule as a purple ribbon in (a) and as a red ribbon in (b). The EF-Tu molecules correspond to the Fig. 2-molecules sharing the same color. Within each molecule, the darkest hue is used for the N-terminal domain (domain 1) and the lightest hue for the C-terminal domain (domain 3). The GDP is represented by a stick model and the Mg2+ ion by a sphere and are colored differently in each EF-Tu molecule. The amino-acid side chains which participate in dimer interactions are shown as stick models. (a) The homologous dimer interactions within 3.5 Å formed between domain 2 of each EF-Tu molecule are shown. The interactions involve the side chains of residues Ser221, Arg223, Glu259, Leu264, Leu265, Asp266, Glu267, Arg269, Glu272 and Leu277 found on loops and a -strand of each EF-Tu molecule. (b) The heterologous dimer interaction formed between domain 1 of EF-Tu and domain 2 of its symmetry-related neighbor is shown. The interactions within 3.5 Å are formed between residues Glu144, Glu147, Leu148, Met151, Arg154, Glu155, Gln159, Gln165 and Asp166 extended from a helix and loop in domain 1 of one EF-Tu-MgGDP molecule and residues Glu215, Asp216, Phe218, Ser219, Ile220, Ser221, Val226, Glu259, Phe261, Arg283 and Arg288 extended from a short -strand and loops in domain 2 of the neighboring molecule. The images were created using MOLSCRIPT (Kraulis, 1991[Kraulis, P. J. (1991). J. Appl. Cryst. 24, 946-950.]) and RASTER3D (Merritt & Bacon, 1997[Merritt, E. A. & Bacon, D. J. (1997). Methods Enzymol. 277, 505-524.]).

The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2006, 62, 433-438) copyright 2006.

Figure was selected by an automated process.