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| | <StructureSection load='1pfv' size='340' side='right'caption='[[1pfv]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='1pfv' size='340' side='right'caption='[[1pfv]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1pfv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PFV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1PFV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1pfv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PFV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2FM:S-(DIFLUOROMETHYL)HOMOCYSTEINE'>2FM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1p7p|1p7p]], [[1pfu|1pfu]], [[1pfw|1pfw]], [[1pfy|1pfy]], [[1pg0|1pg0]], [[1pg2|1pg2]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2FM:S-(DIFLUOROMETHYL)HOMOCYSTEINE'>2FM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">METG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1pfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pfv OCA], [https://pdbe.org/1pfv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pfv RCSB], [https://www.ebi.ac.uk/pdbsum/1pfv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pfv ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1pfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pfv OCA], [http://pdbe.org/1pfv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pfv RCSB], [http://www.ebi.ac.uk/pdbsum/1pfv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pfv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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] | + | [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] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Methionine--tRNA ligase]]
| + | [[Category: Blanquet S]] |
| - | [[Category: Blanquet, S]] | + | [[Category: Crepin T]] |
| - | [[Category: Crepin, T]] | + | [[Category: Honek JF]] |
| - | [[Category: Honek, J F]] | + | [[Category: Mechulam Y]] |
| - | [[Category: Mechulam, Y]] | + | [[Category: Sampson PB]] |
| - | [[Category: Sampson, P B]] | + | [[Category: Schmitt E]] |
| - | [[Category: Schmitt, E]] | + | [[Category: Vaughan MD]] |
| - | [[Category: Vaughan, M D]] | + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
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]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Binding of methionine to methionyl-tRNA synthetase (MetRS) is known to promote conformational changes within the active site. However, the contribution of these rearrangements to enzyme catalysis is not fully understood. In this study, several methionine and methionyl adenylate analogues were diffused into crystals of the monomeric form of Escherichia coli methionyl-tRNA synthetase. The structures of the corresponding complexes were solved at resolutions below 1.9A and compared to those of the enzyme free or complexed with methionine. Residues Y15 and W253 play key roles in the strength of the binding of the amino acid and of its analogues. Indeed, full motions of these residues are required to recover the maximum in free energy of binding. Residue Y15 also controls the size of the hydrophobic pocket where the amino acid side-chain interacts. H301 appears to participate to the specific recognition of the sulphur atom of methionine. Complexes with methionyl adenylate analogues illustrate the shielding by MetRS of the region joining the methionine and adenosine moieties. Finally, the structure of MetRS complexed to a methionine analogue mimicking the tetrahedral carbon of the transition state in the aminoacylation reaction was solved. On the basis of this model, we propose that, in response to the binding of the 3'-end of tRNA, Y15 moves again in order to deshield the anhydride bond in the natural adenylate.
Use of analogues of methionine and methionyl adenylate to sample conformational changes during catalysis in Escherichia coli methionyl-tRNA synthetase.,Crepin T, Schmitt E, Mechulam Y, Sampson PB, Vaughan MD, Honek JF, Blanquet S J Mol Biol. 2003 Sep 5;332(1):59-72. PMID:12946347[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Crepin T, Schmitt E, Mechulam Y, Sampson PB, Vaughan MD, Honek JF, Blanquet S. Use of analogues of methionine and methionyl adenylate to sample conformational changes during catalysis in Escherichia coli methionyl-tRNA synthetase. J Mol Biol. 2003 Sep 5;332(1):59-72. PMID:12946347
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