1f4l: Difference between revisions

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[[Image:1f4l.jpg|left|200px]]


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==CRYSTAL STRUCTURE OF THE E.COLI METHIONYL-TRNA SYNTHETASE COMPLEXED WITH METHIONINE==
The line below this paragraph, containing "STRUCTURE_1f4l", creates the "Structure Box" on the page.
<StructureSection load='1f4l' size='340' side='right'caption='[[1f4l]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
{{STRUCTURE_1f4l| PDB=1f4l |  SCENE= }}
<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>
</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]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f4/1f4l_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>


'''CRYSTAL STRUCTURE OF THE E.COLI METHIONYL-TRNA SYNTHETASE COMPLEXED WITH METHIONINE'''
==See Also==
 
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
 
==About this Structure==
1F4L 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=1F4L OCA].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/11243794 11243794]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Methionine--tRNA ligase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Chonowski T]]
[[Category: Chonowski, T.]]
[[Category: Hervouet N]]
[[Category: Hervouet, N.]]
[[Category: Serre L]]
[[Category: Serre, L.]]
[[Category: Verdon G]]
[[Category: Verdon, G.]]
[[Category: Zelwer C]]
[[Category: Zelwer, C.]]
[[Category: Amino acid]]
[[Category: Rossman fold]]
[[Category: Trna]]
[[Category: Zinc domain]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:53:32 2008''

Latest revision as of 16:23, 13 March 2024

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

Structural highlights

1f4l is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.85Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

1f4l, resolution 1.85Å

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