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PDBsum entry 2fx3
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References listed in PDB file
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Key reference
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Title
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Solving the structure of escherichia coli elongation factor tu using a twinned data set.
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Authors
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S.E.Heffron,
R.Moeller,
F.Jurnak.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2006,
62,
433-438.
[DOI no: ]
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PubMed id
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Abstract
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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.
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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.]).
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The above figure is
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2006,
62,
433-438)
copyright 2006.
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