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New page: left|200px<br /><applet load="1mea" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mea" /> '''METHIONYL-TRNA SYNTHETASE ZINC BINDING DOMAI...
 
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[[Image:1mea.jpg|left|200px]]<br /><applet load="1mea" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1mea" />
'''METHIONYL-TRNA SYNTHETASE ZINC BINDING DOMAIN. 3D STRUCTURE AND HOMOLOGY WITH RUBREDOXIN AND GAG RETROVIRAL PROTEINS'''<br />


==Overview==
==METHIONYL-TRNA SYNTHETASE ZINC BINDING DOMAIN. 3D STRUCTURE AND HOMOLOGY WITH RUBREDOXIN AND GAG RETROVIRAL PROTEINS==
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.
<StructureSection load='1mea' size='340' side='right'caption='[[1mea]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1mea]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MEA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mea OCA], [https://pdbe.org/1mea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mea RCSB], [https://www.ebi.ac.uk/pdbsum/1mea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mea ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SYM_ECOLI SYM_ECOLI] Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.[HAMAP-Rule:MF_00098]


==About this Structure==
==See Also==
1MEA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Methionine--tRNA_ligase Methionine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.10 6.1.1.10] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MEA OCA].
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8515466 8515466]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Methionine--tRNA ligase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Dardel F]]
[[Category: Dardel, F.]]
[[Category: Fourmy D]]
[[Category: Fourmy, D.]]
[[Category: ZN]]
[[Category: aminoacyl-trna synthase]]
 
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