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| - | [[Image:1mea.jpg|left|200px]] | |
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| - | {{Structure
| + | ==METHIONYL-TRNA SYNTHETASE ZINC BINDING DOMAIN. 3D STRUCTURE AND HOMOLOGY WITH RUBREDOXIN AND GAG RETROVIRAL PROTEINS== |
| - | |PDB= 1mea |SIZE=350|CAPTION= <scene name='initialview01'>1mea</scene>
| + | <StructureSection load='1mea' size='340' side='right'caption='[[1mea]]' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
| + | <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> |
| - | |ACTIVITY= <span class='plainlinks'>[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] </span>
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | |GENE= GAG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
| + | <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> |
| - | |DOMAIN= | + | <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> |
| - | |RELATEDENTRY=[[1med|1MED]]
| + | </table> |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mea OCA], [http://www.ebi.ac.uk/pdbsum/1mea PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mea RCSB]</span>
| + | == 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] |
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| - | '''METHIONYL-TRNA SYNTHETASE ZINC BINDING DOMAIN. 3D STRUCTURE AND HOMOLOGY WITH RUBREDOXIN AND GAG RETROVIRAL PROTEINS'''
| + | ==See Also== |
| - | | + | *[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] |
| - | | + | __TOC__ |
| - | ==Overview== | + | </StructureSection> |
| - | 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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| - | | + | |
| - | ==About this Structure==
| + | |
| - | 1MEA 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=1MEA OCA].
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| - | | + | |
| - | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/8515466 8515466]
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| | [[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: aminoacyl-trna synthase]]
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| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:15:04 2008''
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