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Journal Article

Low resolution structure of partially trypsin-degraded polypeptide elongation factor, EF-TU, from Escherichia coli

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons93650

Kabsch,  Wolfgang
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons123190

Schulz,  Georg E.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Kabsch, W., Gast, W. H., Schulz, G. E., & Lebermann, R. (1977). Low resolution structure of partially trypsin-degraded polypeptide elongation factor, EF-TU, from Escherichia coli. Journal of Molecular Biology (London), 117(4), 999-1012. doi:10.1016/S0022-2836(77)80009-0.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-B11C-E
Abstract
The low resolution structure of a trypsin-modified form of elongation factor EF-Tu from Escherichia coli has been determined by X-ray crystallographic methods. The crystals belong to space group P212121 with two molecules in the asymmetric unit. The phase determination was based on three isomorphous heavy-atom derivatives. The quality of the resulting electron density map at 6 Å was sufficient to identify the molecules. The two molecules in the asymmetric unit are related by a non-crystallographic 2-fold rotation. A molecular model was derived by averaging the electron density of the two molecules at equivalent points. Its overall dimensions are 75 Å × 50 Å × 35 Å. The molecule consists of a compact globular head of dimensions 45 Å × 40 Å × 40 Å and a curled tail of diameter 25 Å and length 55 Å. There is a second connection between head and tail, probably an α-helix, such that the molecule forms a ring. The large groove in the centre could accommodate a RNA double helix. The head has a high α-helical content whereas the tail seems to be helix-free. A molecular weight of 43,000 was derived from the electron density map indicating that no major part of the molecule is missing. Possible interactions between EF-Tu and transfer RNA are discussed.