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
| Line 4: | Line 4: | ||
|PDB= 1f4l |SIZE=350|CAPTION= <scene name='initialview01'>1f4l</scene>, resolution 1.85Å | |PDB= 1f4l |SIZE=350|CAPTION= <scene name='initialview01'>1f4l</scene>, resolution 1.85Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=MET:METHIONINE'>MET</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= SYNTHETIC GENE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= SYNTHETIC GENE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1qqt|1QQT]], [[1a8h|1A8H]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f4l OCA], [http://www.ebi.ac.uk/pdbsum/1f4l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f4l RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Verdon, G.]] | [[Category: Verdon, G.]] | ||
[[Category: zelwer, C.]] | [[Category: zelwer, C.]] | ||
| - | [[Category: MET]] | ||
| - | [[Category: ZN]] | ||
[[Category: amino acid]] | [[Category: amino acid]] | ||
[[Category: rossman fold]] | [[Category: rossman fold]] | ||
| Line 35: | Line 36: | ||
[[Category: zinc domain]] | [[Category: zinc domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:15:44 2008'' |
Revision as of 17:15, 30 March 2008
| |||||||
| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | SYNTHETIC GENE (Escherichia coli) | ||||||
| Activity: | Methionine--tRNA ligase, with EC number 6.1.1.10 | ||||||
| Related: | 1QQT, 1A8H
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
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 Sun Mar 30 20:15:44 2008
