7MQL
AAC(3)-IIIa in complex with CoA and neomycin
Summary for 7MQL
| Entry DOI | 10.2210/pdb7mql/pdb |
| Descriptor | Aminoglycoside N(3)-acetyltransferase III, COENZYME A, RIBOSTAMYCIN, ... (5 entities in total) |
| Functional Keywords | antibiotic resistance, aminoglycoside, acetyltransferase, transferase |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 4 |
| Total formula weight | 125048.00 |
| Authors | Zielinski, M.,Berghuis, A.M. (deposition date: 2021-05-05, release date: 2022-07-06, Last modification date: 2024-10-09) |
| Primary citation | Zielinski, M.,Blanchet, J.,Hailemariam, S.,Berghuis, A.M. Structural elucidation of substrate-bound aminoglycoside acetyltransferase (3)-IIIa. Plos One, 17:e0269684-e0269684, 2022 Cited by PubMed Abstract: Canonical aminoglycosides are a large group of antibiotics, where the part of chemical diversity stems from the substitution of the neamine ring system on positions 5 and 6. Certain aminoglycoside modifying enzymes can modify a broad range of 4,5- and 4,6-disubstituted aminoglycosides, with some as many as 15. This study presents the structural and kinetic results describing a promiscuous aminoglycoside acetyltransferase AAC(3)-IIIa. This enzyme has been crystallized in ternary complex with coenzyme A and 4,5- and 4,6-disubstituted aminoglycosides. We have followed up this work with kinetic characterization utilizing a panel of diverse aminoglycosides, including a next-generation aminoglycoside, plazomicin. Lastly, we observed an alternative binding mode of gentamicin in the aminoglycoside binding site, which was proven to be a crystallographic artifact based on mutagenesis. PubMed: 35921328DOI: 10.1371/journal.pone.0269684 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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