3CPW
The structure of the antibiotic LINEZOLID bound to the large ribosomal subunit of HALOARCULA MARISMORTUI
Summary for 3CPW
Entry DOI | 10.2210/pdb3cpw/pdb |
Descriptor | 23S RIBOSOMAL RNA, 50S ribosomal protein L10e, 50S ribosomal protein L13P, ... (40 entities in total) |
Functional Keywords | linezolid, 50s ribosomal subunit, antibiotic complexes, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, trna-binding, metal-binding, zinc-finger, ribosome |
Biological source | HALOARCULA MARISMORTUI More |
Cellular location | Cytoplasm : P12743 |
Total number of polymer chains | 31 |
Total formula weight | 1474423.98 |
Authors | Ippolito, J.A.,Kanyo, Z.K.,Wang, D.,Franceschi, F.J.,Moore, P.B.,Steitz, T.A.,Duffy, E.M. (deposition date: 2008-04-01, release date: 2008-07-22, Last modification date: 2024-02-21) |
Primary citation | Ippolito, J.A.,Kanyo, Z.K.,Wang, D.,Franceschi, F.J.,Moore, P.B.,Steitz, T.A.,Duffy, E.M. Crystal Structure of the Oxazolidinone Antibiotic Linezolid Bound to the 50S Ribosomal Subunit J.Med.Chem., 51:3353-3356, 2008 Cited by PubMed Abstract: The oxazolidinone antibacterials target the 50S subunit of prokaryotic ribosomes. To gain insight into their mechanism of action, the crystal structure of the canonical oxazolidinone, linezolid, has been determined bound to the Haloarcula marismortui 50S subunit. Linezolid binds the 50S A-site, near the catalytic center, which suggests that inhibition involves competition with incoming A-site substrates. These results provide a structural basis for the discovery of improved oxazolidinones active against emerging drug-resistant clinical strains. PubMed: 18494460DOI: 10.1021/jm800379d PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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