Analysis and crystallization of a 25 kDa C-terminal fragment of cloned elongation factor Ts from Escherichia coli

A 25 kDa C-terminal tryptic fragment of elongation factor Ts has been purified to homogeneity. Experimental evidence suggests that the 25 kDa C-terminal and the 5.3 kDa N-terminal fragments are structurally independent domains. The N-terminal fragment is shown to be essential for the nucleotide exch...

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Bibliographic Details
Published in:FEBS letters 1995-07, Vol.368 (1), p.49-54
Main Authors: Bøgestrand, Søren, Wiborg, Ove, Thirup, Søren, Nyborg, Jens
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino Acids - analysis
Base Sequence
Cloning, Molecular
Crystallization
Crystallography, X-Ray
DNA Primers
Elongation factor Ts
Escherichia coli
Escherichia coli - chemistry
Escherichia coli - genetics
Mass Spectrometry
Molecular Sequence Data
Nucleotide exchange factor
Peptide Elongation Factors - chemistry
Peptide Elongation Factors - genetics
Protein biosynthesis
Protein Conformation
Pseudo symmetry
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Trypsin
Trypsin fragments
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Summary:A 25 kDa C-terminal tryptic fragment of elongation factor Ts has been purified to homogeneity. Experimental evidence suggests that the 25 kDa C-terminal and the 5.3 kDa N-terminal fragments are structurally independent domains. The N-terminal fragment is shown to be essential for the nucleotide exchange activity. Crystals of the C-terminal fragment belong to space group P2 or P2 1. The diffraction pattern shows a pronounced pseudo-C2 symmetry at low resolution. This pseudo symmetry increases when the crystals are irradiated with X-rays for a few hours.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(95)00597-3