1f4l

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{{STRUCTURE_1f4l| PDB=1f4l | SCENE= }}
{{STRUCTURE_1f4l| PDB=1f4l | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE E.COLI METHIONYL-TRNA SYNTHETASE COMPLEXED WITH METHIONINE'''
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===CRYSTAL STRUCTURE OF THE E.COLI METHIONYL-TRNA SYNTHETASE COMPLEXED WITH METHIONINE===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 11243794 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11243794}}
==About this Structure==
==About this Structure==
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[[Category: Trna]]
[[Category: Trna]]
[[Category: Zinc domain]]
[[Category: Zinc domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:53:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:40:56 2008''

Revision as of 23:40, 30 June 2008

Template:STRUCTURE 1f4l

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

Template:ABSTRACT PUBMED 11243794

About this Structure

1F4L is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from 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:11243794

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