6SPN
Structure of the Escherichia coli methionyl-tRNA synthetase complexed with beta-methionine
Summary for 6SPN
| Entry DOI | 10.2210/pdb6spn/pdb |
| Related | 1QQT |
| Descriptor | Methionine--tRNA ligase, ZINC ION, CITRIC ACID, ... (6 entities in total) |
| Functional Keywords | trna aminoacylation, translation |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 65406.11 |
| Authors | Nigro, G.,Schmitt, E.,Mechulam, Y. (deposition date: 2019-09-02, release date: 2020-01-01, Last modification date: 2023-11-15) |
| Primary citation | Nigro, G.,Bourcier, S.,Lazennec-Schurdevin, C.,Schmitt, E.,Marliere, P.,Mechulam, Y. Use of beta3-methionine as an amino acid substrate of Escherichia coli methionyl-tRNA synthetase. J.Struct.Biol., 209:107435-107435, 2020 Cited by PubMed Abstract: Polypeptides containing β-amino acids are attractive tools for the design of novel proteins having unique properties of medical or industrial interest. Incorporation of β-amino acids in vivo requires the development of efficient aminoacyl-tRNA synthetases specific of these non-canonical amino acids. Here, we have performed a detailed structural and biochemical study of the recognition and use of β-Met by Escherichia coli methionyl-tRNA synthetase (MetRS). We show that MetRS binds β-Met with a 24-fold lower affinity but catalyzes the esterification of the non-canonical amino acid onto tRNA with a rate lowered by three orders of magnitude. Accurate measurements of the catalytic parameters required careful consideration of the presence of contaminating α-Met in β-Met commercial samples. The 1.45 Å crystal structure of the MetRS: β-Met complex shows that β-Met binds the enzyme essentially like α-Met, but the carboxylate moiety is mobile and not adequately positioned to react with ATP for aminoacyl adenylate formation. This study provides structural and biochemical bases for engineering MetRS with improved β-Met aminoacylation capabilities. PubMed: 31862305DOI: 10.1016/j.jsb.2019.107435 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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