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Structure–Function Relationship of Aminopeptidase P fromPseudomonas aeruginosa

  • [设施]:上海设施
  • [期刊/会议名称]:Frontiers in Microbiology
  • [摘要]:PepP is a virulence-associated gene in Pseudomonas aeruginosa, making it an attractive target for anti-P. aeruginosa drug development. The encoded protein, aminopeptidases P (Pa-PepP), is a type of X-prolyl peptidase that possesses diverse biological functions. The crystal structure verified its canonical pita-bread fold and functional tetrameric assembly, and the functional studies measured the influences of different metal ions on the activity. A trimetal manganese cluster was observed at the active site, elucidating the mechanism of inhibition by metal ions. Additionally, a loop extending from the active site appeared to be important for specific large-substrate binding. Based on the structural comparison and bacterial invasion assays, we showed that this non-conserved surface loop was critical for P. aeruginosa virulence. Taken together, these findings can extend our understanding of the catalytic mechanism and virulence-related functions of Pa-PepP and provide a solid foundation for the design of specific inhibitors against pathogenic-bacterial infections.
  • [发表日期]:2017
  • [第一作者]: CT Peng
  • [第一作者单位]: State Key Laboratory of Biotherapy
  • [通讯作者]:Rui Bao
  • [通讯作者单位]: State Key Laboratory of Biotherapy
  • [论文类型]:0
  • [期刊分类]:SCI2区
  • [学科分类]:微生物学
  • [影响因子]:4.076
  • [关键词]:Pseudomonas aeruginosa, aminopeptidase P, virulence, tri-nuclear form, X-ray crystallography
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