2X1L
Crystal structure of Mycobacterium smegmatis methionyl-tRNA synthetase in complex with methionine and adenosine
Summary for 2X1L
| Entry DOI | 10.2210/pdb2x1l/pdb |
| Related | 2X1M |
| Descriptor | METHIONYL-TRNA SYNTHETASE, METHIONINE, ADENOSINE, ... (6 entities in total) |
| Functional Keywords | nucleotide-binding, protein biosynthesis, ligase, aminoacyl-trna synthetase |
| Biological source | MYCOBACTERIUM SMEGMATIS |
| Total number of polymer chains | 3 |
| Total formula weight | 179729.91 |
| Authors | Ingvarsson, H.,Jones, T.A.,Unge, T. (deposition date: 2009-12-31, release date: 2010-07-28, Last modification date: 2023-12-20) |
| Primary citation | Ingvarsson, H.,Unge, T. Flexibility and Communication within the Structure of the Mycobacterium Smegmatis Methionyl-tRNA Synthetase. FEBS J., 277:3947-, 2010 Cited by PubMed Abstract: Two structures of monomeric methionyl-tRNA synthetase, from Mycobacterium smegmatis, in complex with the ligands methionine/adenosine and methionine, were analyzed by X-ray crystallography at 2.3 Å and at 2.8 Å, respectively. The structures demonstrated the flexibility of the multidomain enzyme. A new conformation of the structure was identified in which the connective peptide domain bound more closely to the catalytic domain than described previously. The KMSKS(301-305) loop in our structures was in an open and inactive conformation that differed from previous structures by a rotation of the loop of about 90° around hinges located at Asn297 and Val310. The binding of adenosine to the methionyl-tRNA synthetase methionine complex caused a shift in the KMSKS domain that brought it closer to the catalytic domain. The potential use of the adenosine-binding site for inhibitor binding was evaluated and a potential binding site for a specific allosteric inhibitor was identified. PubMed: 20796028DOI: 10.1111/J.1742-4658.2010.07784.X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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