Structural highlights
Function
[SYM_ECOLI] Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.[HAMAP-Rule:MF_00098]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of Escherichia coli methionyl-tRNA synthetase highlights species-specific features.,Mechulam Y, Schmitt E, Maveyraud L, Zelwer C, Nureki O, Yokoyama S, Konno M, Blanquet S J Mol Biol. 1999 Dec 17;294(5):1287-97. PMID:10600385[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mechulam Y, Schmitt E, Maveyraud L, Zelwer C, Nureki O, Yokoyama S, Konno M, Blanquet S. Crystal structure of Escherichia coli methionyl-tRNA synthetase highlights species-specific features. J Mol Biol. 1999 Dec 17;294(5):1287-97. PMID:10600385 doi:10.1006/jmbi.1999.3339
