1med

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{{STRUCTURE_1med| PDB=1med | SCENE= }}
{{STRUCTURE_1med| PDB=1med | SCENE= }}
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'''METHIONYL-TRNA SYNTHETASE ZINC BINDING DOMAIN. 3D STRUCTURE AND HOMOLOGY WITH RUBREDOXIN AND GAG RETROVIRAL PROTEINS'''
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===METHIONYL-TRNA SYNTHETASE ZINC BINDING DOMAIN. 3D STRUCTURE AND HOMOLOGY WITH RUBREDOXIN AND GAG RETROVIRAL PROTEINS===
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==Overview==
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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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The line below this paragraph, {{ABSTRACT_PUBMED_8515466}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 8515466 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8515466}}
==About this Structure==
==About this Structure==
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1MED is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MED OCA].
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1MED is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MED OCA].
==Reference==
==Reference==
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[[Category: Fourmy, D.]]
[[Category: Fourmy, D.]]
[[Category: Aminoacyl-trna synthase]]
[[Category: Aminoacyl-trna synthase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:56:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:47:18 2008''

Revision as of 20:47, 2 July 2008

Image:1med.png

Template:STRUCTURE 1med

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

Template:ABSTRACT PUBMED 8515466

About this Structure

1MED is a Single protein structure of sequence from Escherichia coli. Full experimental 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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