Crystal structure of mannose specific IIA subunit of phosphotransferase system from streptococcus pneumoniae

Malgorzata Magoch, Przemyslaw Nogly, Przemyslaw Grudnik, Pikyee Ma, Bozena Boczkus, Ana Rute Neves, Margarida Archer, Grzegorz Dubin

Research output: Contribution to journalArticlepeer-review

Abstract

Streptococcus pneumoniae is a frequent bacterial pathogen of the human respiratory tract causing pneumonia, meningitis and sepsis, a serious healthcare burden in all age groups. S. pneumoniae lacks complete respiratory chain and relies on carbohydrate fermentation for energy generation. One of the essential components for this includes the mannose phosphotransferase system (Man-PTS), which plays a central role in glucose transport and exhibits a broad specificity for a range of hexoses. Importantly, Man-PTS is involved in the global regulation of gene expression for virulence determinants. We herein report the three-dimensional structure of the EIIA domain of S. pneumoniae mannose phosphotransferase system (SpEIIA-Man). Our structure shows a dimeric arrangement of EIIA and reveals a detailed molecular description of the active site. Since PTS transporters are exclusively present in microbes and sugar transporters have already been suggested as valid targets for antistreptococcal antibiotics, our work sets foundation for the future development of antimicrobial strategies against Streptococcus pneumoniae.

Original languageEnglish
Article number4633
JournalMolecules
Volume25
Issue number20
DOIs
Publication statusPublished - Oct 2020

Keywords

  • IIA subunit
  • Mannose PTS
  • Phosphotransferase system
  • Streptococcus pneumoniae
  • Sugar transport
  • X-ray crystallography

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