6MB5
AAC-IIIb binary with NEOMYCIN
Summary for 6MB5
| Entry DOI | 10.2210/pdb6mb5/pdb |
| Descriptor | Aac(3)-IIIb protein, NEOMYCIN (3 entities in total) |
| Functional Keywords | acetyltransferase, promiscuity, gnat, antibiotic resistance, antibiotic, transferase-antibiotic complex, transferase/antibiotic |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 1 |
| Total formula weight | 29633.44 |
| Authors | Cuneo, M.J.,Kumar, P. (deposition date: 2018-08-29, release date: 2018-11-07, Last modification date: 2024-03-13) |
| Primary citation | Kumar, P.,Selvaraj, B.,Serpersu, E.H.,Cuneo, M.J. Encoding of Promiscuity in an Aminoglycoside Acetyltransferase. J. Med. Chem., 61:10218-10227, 2018 Cited by PubMed Abstract: Aminoglycoside antibiotics are a large family of antibiotics that can be divided into two distinct classes on the basis of the substitution pattern of the central deoxystreptamine ring. Although aminoglycosides are chemically, structurally, and topologically diverse, some aminoglycoside-modifying enzymes (AGMEs) are able to inactivate as many as 15 aminoglycosides from the two main classes, the kanamycin- and neomycin-based antibiotics. Here, we present the crystal structure of a promiscuous AGME, aminoglycoside- N3-acetyltransferase-IIIb (AAC-IIIb), in the apo form, in binary drug (sisomicin, neomycin, and paromomycin) and coenzyme A (CoASH) complexes, and in the ternary neomycin-CoASH complex. These data provide a structural framework for interpretation of the thermodynamics of enzyme-ligand interactions and the role of solvent in the recognition of ligands. In combination with the recent structure of an AGME that does not have broad substrate specificity, these structures allow for the direct determination of how antibiotic promiscuity is encoded in some AGMEs. PubMed: 30347146DOI: 10.1021/acs.jmedchem.8b01393 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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