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1f4l

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(New page: 200px<br /><applet load="1f4l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f4l, resolution 1.85&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1f4l.jpg|left|200px]]<br /><applet load="1f4l" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1f4l, resolution 1.85&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE E.COLI METHIONYL-TRNA SYNTHETASE COMPLEXED WITH METHIONINE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE E.COLI METHIONYL-TRNA SYNTHETASE COMPLEXED WITH METHIONINE==
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Amino acid selection by aminoacyl-tRNA synthetases requires efficient, mechanisms to avoid incorrect charging of the cognate tRNAs. A, proofreading mechanism prevents Escherichia coli methionyl-tRNA synthetase, (EcMet-RS) from activating in vivo L-homocysteine, a natural competitor of, L-methionine recognised by the enzyme. The crystal structure of the, complex between EcMet-RS and L-methionine solved at 1.8 A resolution, exhibits some conspicuous differences with the recently published free, enzyme structure. Thus, the methionine delta-sulphur atom replaces a water, molecule H-bonded to Leu13N and Tyr260O(eta) in the free enzyme., Rearrangements of aromatic residues enable the protein to form a, hydrophobic pocket around the ligand side-chain. The subsequent formation, of an extended water molecule network contributes to relative, displacements, up to 3 A, of several domains of the protein. The structure, of this complex supports a plausible mechanism for the selection of, L-methionine versus L-homocysteine and suggests the possibility of, information transfer between the different functional domains of the, enzyme.
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<StructureSection load='1f4l' size='340' side='right'caption='[[1f4l]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1f4l]] 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=1F4L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F4L FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MET:METHIONINE'>MET</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f4l OCA], [https://pdbe.org/1f4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f4l RCSB], [https://www.ebi.ac.uk/pdbsum/1f4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f4l ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f4/1f4l_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f4l ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1F4L 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 and MET as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1F4L OCA].
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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How methionyl-tRNA synthetase creates its amino acid recognition pocket upon L-methionine binding., Serre L, Verdon G, Choinowski T, Hervouet N, Risler JL, Zelwer C, J Mol Biol. 2001 Mar 2;306(4):863-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11243794 11243794]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Methionine--tRNA ligase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Chonowski T]]
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[[Category: Chonowski, T.]]
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[[Category: Hervouet N]]
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[[Category: Hervouet, N.]]
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[[Category: Serre L]]
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[[Category: Serre, L.]]
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[[Category: Verdon G]]
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[[Category: Verdon, G.]]
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[[Category: Zelwer C]]
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[[Category: zelwer, C.]]
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[[Category: MET]]
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[[Category: ZN]]
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[[Category: amino acid]]
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[[Category: rossman fold]]
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[[Category: trna]]
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[[Category: zinc domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:36:41 2007''
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Current revision

CRYSTAL STRUCTURE OF THE E.COLI METHIONYL-TRNA SYNTHETASE COMPLEXED WITH METHIONINE

PDB ID 1f4l

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