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© Structural Dynamics Of Macromolecules
The structure of a bacterial analog of the nicotinic receptor (one color per subunit) inserted into the cell membrane (grey and orange). A representation of the volume accessible to ions is shown in yellow.
Publication : Eur. J. Biochem.

Three-dimensional structure of phenylalanyl-transfer RNA synthetase from Thermus thermophilus HB8 at 0.6- nm resolution.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Eur. J. Biochem. - 01 Sep 1992

Reshetnikova L, Chernaya M, Ankilova V, Lavrik O, Delarue M, Thierry JC, Moras D, Safro M.

Link to Pubmed [PMID] – 1521534

Link to DOI – 10.1111/j.1432-1033.1992.tb17202.x

Eur J Biochem. 1992 Sep 1;208(2):411-7.

The three-dimensional structure of the heterodimeric alpha 2 beta 2 enzyme phenylalanyl-tRNA synthetase from Thermus thermophilus HB8 has been determined by X-ray crystallography, using the multiple-isomorphous-replacement method at 0.6 nm resolution. Trigonal crystals of space group P3(2)21 have cell dimensions a = b = 17.6 nm and c = 14.2 nm. Assuming one heterodimeric molecule/asymmetric unit, the ratio of unit cell volume/molecular mass was V = 0.00244 nm3/Da, which is in the middle of the range normally observed. However, after a rotation-function calculation and measurement of the density of the native crystals, we postulate the existence of only the alpha beta dimer in the asymmetric units. This implies 73% solvent content in the unit cell. Three heavy-atom derivatives [K2PtCl4, KAu(CN)2 and Hg(CH3COO)2] and the solvent-flattening procedure were used for electron-density-map calculations. This map confirmed our hypothesis and revealed a remarkably large space filled by solvent, with alpha beta dimer only in the asymmetric unit. The phenylalanyl-tRNA synthetase from T. thermophilus molecule has a ‘quasi-linear’ subunit organization. As can be concluded at this level of resolution, there is no contact between small alpha subunits in the functional heterodimer.