1QQT
METHIONYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI
Summary for 1QQT
Entry DOI | 10.2210/pdb1qqt/pdb |
Descriptor | METHIONYL-TRNA SYNTHETASE, ZINC ION (3 entities in total) |
Functional Keywords | rossmann fold, helix bundle, trna ligase, ligase |
Biological source | Escherichia coli |
Cellular location | Cytoplasm: P00959 |
Total number of polymer chains | 1 |
Total formula weight | 62908.43 |
Authors | Mechulam, Y.,Schmitt, E.,Maveyraud, L.,Zelwer, C.,Nureki, O.,Yokoyama, S.,Konno, M.,Blanquet, S. (deposition date: 1999-06-08, release date: 2000-01-01, Last modification date: 2024-02-14) |
Primary citation | 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., 294:1287-1297, 1999 Cited by PubMed 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. PubMed: 10600385DOI: 10.1006/jmbi.1999.3339 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.03 Å) |
Structure validation
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