Crystal structure of Escherichia coli methionyl-tRNA synthetase highlights species-specific features.

Yves Mechulam 1 Emmanuelle Schmitt 1 Laurent Maveyraud 1 Charles Zelwer 2 Osamu Nureki 3 Shigeyuki Yokoyama Michiko Konno 4 Sylvain Blanquet 1, *
* Corresponding author
1 BIOC - Laboratoire de Biochimie de l'Ecole polytechnique
2 CBM - Centre de biophysique moléculaire
3 DBI - Department of biological information-Tokyo Institute of Technology
4 Department of Chemistry
Abstract : The 3D structure of monomeric C-truncated Escherichia coli methionyl-tRNA synthetase, a class 1 aminoacyl-tRNA synthetase, has been solved at 2.0 A resolution. Remarkably, the polypeptide connecting the two halves of the Rossmann fold exposes two identical knuckles related by a 2-fold axis but with zinc in the distal knuckle only. Examination of available MetRS orthologs reveals four classes according to the number and zinc content of the putative knuckles. Extreme cases are exemplified by the MetRS of eucaryotic or archaeal origin, where two knuckles and two metal ions are expected, and by the mitochondrial enzymes, which are predicted to have one knuckle without metal ion.
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Submitted on : Wednesday, July 10, 2013 - 4:44:10 PM
Last modification on : Wednesday, March 27, 2019 - 3:56:02 PM

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Yves Mechulam, Emmanuelle Schmitt, Laurent Maveyraud, Charles Zelwer, Osamu Nureki, et al.. Crystal structure of Escherichia coli methionyl-tRNA synthetase highlights species-specific features.. Journal of Molecular Biology, Elsevier, 1999, 294 (5), pp.1287-1297. ⟨10.1006/jmbi.1999.3339⟩. ⟨hal-00841066⟩

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