1mea
From Proteopedia
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METHIONYL-TRNA SYNTHETASE ZINC BINDING DOMAIN. 3D STRUCTURE AND HOMOLOGY WITH RUBREDOXIN AND GAG RETROVIRAL PROTEINS
Overview
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.
About this Structure
1MEA is a Single protein structure of sequence from Escherichia coli with ZN as ligand. Active as Methionine--tRNA ligase, with EC number 6.1.1.10 Full crystallographic information is available from OCA.
Reference
Methionyl-tRNA synthetase zinc binding domain. Three-dimensional structure and homology with rubredoxin and gag retroviral proteins., Fourmy D, Dardel F, Blanquet S, J Mol Biol. 1993 Jun 20;231(4):1078-89. PMID:8515466
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