1f4l: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1f4l.jpg|left|200px]]
{{Seed}}
[[Image:1f4l.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1f4l|  PDB=1f4l  |  SCENE=  }}  
{{STRUCTURE_1f4l|  PDB=1f4l  |  SCENE=  }}  


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




==Overview==
<!--  
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.
The line below this paragraph, {{ABSTRACT_PUBMED_11243794}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11243794 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_11243794}}


==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Trna]]
[[Category: Trna]]
[[Category: Zinc domain]]
[[Category: Zinc domain]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:53:32 2008''
 
''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

File:1f4l.png

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

Page seeded by OCA on Tue Jul 1 02:40:56 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA