This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1f4l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
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

Image: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

Retrieved from "http://52.214.119.220/wiki/index.php/1f4l"
Personal tools