Crystal structure of betaine aldehyde dehydrogenase from Burkholderia pseudomallei

Acta Crystallogr F Struct Biol Commun. 2022 Feb 1;78(Pt 2):45-51. doi: 10.1107/S2053230X21013455. Epub 2022 Jan 27.

Abstract

Burkholderia pseudomallei infection causes melioidosis, which is often fatal if untreated. There is a need to develop new and more effective treatments for melioidosis. This study reports apo and cofactor-bound crystal structures of the potential drug target betaine aldehyde dehydrogenase (BADH) from B. pseudomallei. A structural comparison identified similarities to BADH from Pseudomonas aeruginosa which is inhibited by the drug disulfiram. This preliminary analysis could facilitate drug-repurposing studies for B. pseudomallei.

Keywords: Burkholderia pseudomallei; betaine aldehyde dehydrogenase; disulfiram; drug repurposing; inhibition; melioidosis.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Betaine-Aldehyde Dehydrogenase / chemistry*
  • Betaine-Aldehyde Dehydrogenase / genetics
  • Betaine-Aldehyde Dehydrogenase / metabolism
  • Burkholderia pseudomallei / enzymology*
  • Crystallography, X-Ray
  • Models, Molecular
  • Protein Conformation
  • Pseudomonas aeruginosa / enzymology

Substances

  • Bacterial Proteins
  • Betaine-Aldehyde Dehydrogenase