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Atomic-Resolution Structure of a Class C ß-Lactamase and Its Complex with Avibactam.
Pozzi, Cecilia; Di Pisa, Flavio; De Luca, Filomena; Benvenuti, Manuela; Docquier, Jean Denis; Mangani, Stefano.
Afiliación
  • Pozzi C; Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Via Aldo Moro 2, 53100, Siena, Italy.
  • Di Pisa F; Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Via Aldo Moro 2, 53100, Siena, Italy.
  • De Luca F; Department of Medical Biotechnology, University of Siena, Via Aldo Moro 2, 53100, Siena, Italy.
  • Benvenuti M; Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Via Aldo Moro 2, 53100, Siena, Italy.
  • Docquier JD; Department of Medical Biotechnology, University of Siena, Via Aldo Moro 2, 53100, Siena, Italy.
  • Mangani S; Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Via Aldo Moro 2, 53100, Siena, Italy.
ChemMedChem ; 13(14): 1437-1446, 2018 07 18.
Article en En | MEDLINE | ID: mdl-29786960
ß-Lactamases (BLs) are important antibiotic-resistance determinants that significantly compromise the efficacy of valuable ß-lactam antibacterial drugs. Thus, combinations with BL inhibitor were developed. Avibactam is the first non-ß-lactam BL inhibitor introduced into clinical practice. Ceftazidime-avibactam represents one of the few last-resort antibiotics available for the treatment of infections caused by near-pandrug-resistant bacteria. TRU-1 is a chromosomally encoded AmpC-type BL of Aeromonas enteropelogenes, related to the FOX-type BLs and constitutes a good model for class C BLs. TRU-1 crystals provided ultrahigh-resolution diffraction data for the native enzyme and for its complex with avibactam. A comparison of the native and avibactam-bound structures revealed new details in the conformations of residues relevant for substrate and/or inhibitor binding. Furthermore, a comparison of the TRU-1 and Pseudomonas aeruginosa AmpC avibactam-bound structures revealed two inhibitor conformations that were likely to correspond to two different states occurring during inhibitor carbamylation/recyclization.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Beta-Lactamasas / Aeromonas / Compuestos de Azabiciclo Límite: Humans Idioma: En Revista: ChemMedChem Asunto de la revista: FARMACOLOGIA / QUIMICA Año: 2018 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Alemania
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Beta-Lactamasas / Aeromonas / Compuestos de Azabiciclo Límite: Humans Idioma: En Revista: ChemMedChem Asunto de la revista: FARMACOLOGIA / QUIMICA Año: 2018 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Alemania