METHIONYL-TRANSFER RNA-SYNTHETASE ZINC-BINDING DOMAIN - 3-DIMENSIONAL STRUCTURE AND HOMOLOGY WITH RUBREDOXIN AND GAG RETROVIRAL PROTEINS

被引:35
作者
FOURMY, D [1 ]
DARDEL, F [1 ]
BLANQUET, S [1 ]
机构
[1] ECOLE POLYTECH, BIOCHIM LAB, 17K, URA 240, F-91128 PALAISEAU, FRANCE
关键词
NUCLEAR MAGNETIC RESONANCE; ZINC; AMINOACYL-TRANSFER RNA SYNTHETASE; RESTRAINED MOLECULAR DYNAMICS; PEPTIDE;
D O I
10.1006/jmbi.1993.1353
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 AÅ 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. © 1993 Academic Press, Inc.
引用
收藏
页码:1078 / 1089
页数:12
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