1pg2: Difference between revisions

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[[Image:1pg2.gif|left|200px]]<br /><applet load="1pg2" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1pg2.gif|left|200px]]
caption="1pg2, resolution 1.75&Aring;" />
 
'''METHIONYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI COMPLEXED WITH METHIONINE AND ADENOSINE'''<br />
{{Structure
|PDB= 1pg2 |SIZE=350|CAPTION= <scene name='initialview01'>1pg2</scene>, resolution 1.75&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=ADN:ADENOSINE'>ADN</scene> and <scene name='pdbligand=MET:METHIONINE'>MET</scene>
|ACTIVITY= [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]
|GENE= metG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
}}
 
'''METHIONYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI COMPLEXED WITH METHIONINE AND ADENOSINE'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1PG2 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 <scene name='pdbligand=ADN:'>ADN</scene> and <scene name='pdbligand=MET:'>MET</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1PG2 OCA].  
1PG2 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=1PG2 OCA].  


==Reference==
==Reference==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12946347 12946347]
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:[http://www.ncbi.nlm.nih.gov/pubmed/12946347 12946347]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Methionine--tRNA ligase]]
[[Category: Methionine--tRNA ligase]]
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[[Category: rossmann fold]]
[[Category: rossmann fold]]


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Revision as of 14:23, 20 March 2008

File:1pg2.gif


PDB ID 1pg2

Drag the structure with the mouse to rotate
, resolution 1.75Å
Ligands: and
Gene: metG (Escherichia coli)
Activity: Methionine--tRNA ligase, with EC number 6.1.1.10
Coordinates: save as pdb, mmCIF, xml



METHIONYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI COMPLEXED WITH METHIONINE AND ADENOSINE


OverviewOverview

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.

About this StructureAbout this Structure

1PG2 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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

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