1F4L

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

Summary for 1F4L

• Entry DOI: 10.2210/pdb1f4l/pdb
• Related: 1A8H 1QQT
• Descriptor: METHIONYL-TRNA SYNTHETASE, ZINC ION, METHIONINE, ... (4 entities in total)
• Functional Keywords: rossmann fold, zinc domain, amino acid, trna, hydrolase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P00959
• Total number of polymer chains: 1
• Total formula weight: 63174.75

Authors

Serre, L.,Verdon, G.,Chonowski, T.,Hervouet, N.,Zelwer, C. (deposition date: 2000-06-08, release date: 2001-03-21, Last modification date: 2024-03-13)

Primary citation

Serre, L.,Verdon, G.,Choinowski, T.,Hervouet, N.,Risler, J.L.,Zelwer, C.
How methionyl-tRNA synthetase creates its amino acid recognition pocket upon L-methionine binding.
J.Mol.Biol., 306:863-876, 2001

PubMed Abstract: 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.

PubMed: 11243794
DOI: 10.1006/jmbi.2001.4408

Experimental method

X-RAY DIFFRACTION (1.85 Å)