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Crystallographic structure determination and analysis of a potential short-chain dehydrogenase/reductase (SDR) from multi-drug resistant Acinetobacter baumannii.
Ghafoori, Seyed Mohammad; Abdollahpour, Soha; Shirmast, Paniz; Forwood, Jade K.
Afiliação
  • Ghafoori SM; School of Dentistry and Medical Sciences, Charles Sturt University, Wagga, Wagga, NSW, Australia.
  • Abdollahpour S; School of Dentistry and Medical Sciences, Charles Sturt University, Wagga, Wagga, NSW, Australia.
  • Shirmast P; Menzies Health Institute Queensland and School of Medical Sciences, Griffith University, Gold Coast, QLD, Australia.
  • Forwood JK; School of Dentistry and Medical Sciences, Charles Sturt University, Wagga, Wagga, NSW, Australia.
PLoS One ; 18(8): e0289992, 2023.
Article em En | MEDLINE | ID: mdl-37616198
Bacterial antibiotic resistance remains an ever-increasing worldwide problem, requiring new approaches and enzyme targets. Acinetobacter baumannii is recognised as one of the most significant antibiotic-resistant bacteria, capable of carrying up to 45 different resistance genes, and new drug discovery targets for this organism is an urgent priority. Short-chain dehydrogenase/reductase enzymes are a large protein family with >60,000 members involved in numerous biosynthesis pathways. Here, we determined the structure of an SDR protein from A. baumannii and assessed the putative co-factor comparisons with previously co-crystalised enzymes and cofactors. This study provides a basis for future studies to examine these potential co-factors in vitro.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Acinetobacter baumannii Idioma: En Ano de publicação: 2023 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Acinetobacter baumannii Idioma: En Ano de publicação: 2023 Tipo de documento: Article