6R1M
Crystal structure of E. coli seryl-tRNA synthetase complexed to seryl sulfamoyl adenosine
Summary for 6R1M
| Entry DOI | 10.2210/pdb6r1m/pdb |
| Descriptor | Serine--tRNA ligase, 5'-O-(N-(L-SERYL)-SULFAMOYL)ADENOSINE, PHOSPHATE ION, ... (5 entities in total) |
| Functional Keywords | aminoacyl-trna synthetase, class ii, protein synthesis, inhibitor, ligase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 100817.62 |
| Authors | Salimraj, R.,Cain, R.,Roper, D.I. (deposition date: 2019-03-14, release date: 2020-01-22, Last modification date: 2024-01-24) |
| Primary citation | Cain, R.,Salimraj, R.,Punekar, A.S.,Bellini, D.,Fishwick, C.W.G.,Czaplewski, L.,Scott, D.J.,Harris, G.,Dowson, C.G.,Lloyd, A.J.,Roper, D.I. Structure-Guided Enhancement of Selectivity of Chemical Probe Inhibitors Targeting Bacterial Seryl-tRNA Synthetase. J.Med.Chem., 62:9703-9717, 2019 Cited by PubMed Abstract: Aminoacyl-tRNA synthetases are ubiquitous and essential enzymes for protein synthesis and also a variety of other metabolic processes, especially in bacterial species. Bacterial aminoacyl-tRNA synthetases represent attractive and validated targets for antimicrobial drug discovery if issues of prokaryotic versus eukaryotic selectivity and antibiotic resistance generation can be addressed. We have determined high-resolution X-ray crystal structures of the and seryl-tRNA synthetases in complex with aminoacyl adenylate analogues and applied a structure-based drug discovery approach to explore and identify a series of small molecule inhibitors that selectively inhibit bacterial seryl-tRNA synthetases with greater than 2 orders of magnitude compared to their human homologue, demonstrating a route to the selective chemical inhibition of these bacterial targets. PubMed: 31626547DOI: 10.1021/acs.jmedchem.9b01131 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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