1MED

METHIONYL-TRNA SYNTHETASE ZINC BINDING DOMAIN. 3D STRUCTURE AND HOMOLOGY WITH RUBREDOXIN AND GAG RETROVIRAL PROTEINS

Summary for 1MED

• Entry DOI: 10.2210/pdb1med/pdb
• Descriptor: METHIONYL-tRNA SYNTHETASE, ZINC ION (2 entities in total)
• Functional Keywords: aminoacyl-trna synthase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P00959
• Total number of polymer chains: 1
• Total formula weight: 3034.72

Authors

Fourmy, D.,Dardel, F. (deposition date: 1992-11-09, release date: 1993-10-31, Last modification date: 2024-05-01)

Primary citation

Fourmy, D.,Dardel, F.,Blanquet, S.
Methionyl-tRNA synthetase zinc binding domain. Three-dimensional structure and homology with rubredoxin and gag retroviral proteins.
J.Mol.Biol., 231:1078-1089, 1993

PubMed Abstract: Methionyl-tRNA synthetase from Escherichia coli contains one tightly bound zinc atom per subunit. The region encompassing residues 138 to 163 of this enzyme is responsible for the metal binding. A 28-mer peptide corresponding to these residues was expressed in vivo and shown to contain approximately 1 mol of tightly bound Zn/mol of peptide. In this study, the three-dimensional solution structure of this peptide was solved by means of two-dimensional proton NMR spectroscopy. A total of 133 nuclear Overhauser effect distance constraints and 22 dihedral angle restraints were used for the calculations, using a hybrid distance-geometry-simulated annealing strategy. Excluding the first four residues, the resulting structure is well-defined (r.m.s.d. 0.71 A for backbone atoms) and composed of a series of four tight turns. The second and the fourth turns are composed of CXXC sequences which are structurally homologous to the NH-S turns found in the metal binding sites of gag retroviral proteins and rubredoxin. The solution structure of the zinc binding peptide shows significant discrepancies with the crystal structure of methionyl-tRNA synthetase.

PubMed: 8515466
DOI: 10.1006/jmbi.1993.1353

Experimental method

SOLUTION NMR