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rdf:type |
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lifeskim:mentions |
umls-concept:C0025653,
umls-concept:C0033684,
umls-concept:C0035366,
umls-concept:C0035938,
umls-concept:C0328767,
umls-concept:C0450363,
umls-concept:C0678594,
umls-concept:C1148621,
umls-concept:C1325389,
umls-concept:C1334043,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2697616
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pubmed:issue |
4
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pubmed:dateCreated |
1993-7-20
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0022-2836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
231
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1078-89
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8515466-Amino Acid Sequence,
pubmed-meshheading:8515466-Cysteine,
pubmed-meshheading:8515466-Escherichia coli,
pubmed-meshheading:8515466-Gene Products, gag,
pubmed-meshheading:8515466-Magnetic Resonance Spectroscopy,
pubmed-meshheading:8515466-Methionine-tRNA Ligase,
pubmed-meshheading:8515466-Models, Molecular,
pubmed-meshheading:8515466-Molecular Sequence Data,
pubmed-meshheading:8515466-Mutation,
pubmed-meshheading:8515466-Peptide Fragments,
pubmed-meshheading:8515466-Protein Conformation,
pubmed-meshheading:8515466-Protein Precursors,
pubmed-meshheading:8515466-Rubredoxins,
pubmed-meshheading:8515466-Sequence Homology, Amino Acid,
pubmed-meshheading:8515466-Zinc
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pubmed:year |
1993
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pubmed:articleTitle |
Methionyl-tRNA synthetase zinc binding domain. Three-dimensional structure and homology with rubredoxin and gag retroviral proteins.
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pubmed:affiliation |
Laboratoire de Biochimie, URA 240 CNRS Ecole Polytechnique, Palaiseau, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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