TY - JOUR
T1 - Crystal structure of mannose specific IIA subunit of phosphotransferase system from streptococcus pneumoniae
AU - Magoch, Malgorzata
AU - Nogly, Przemyslaw
AU - Grudnik, Przemyslaw
AU - Ma, Pikyee
AU - Boczkus, Bozena
AU - Neves, Ana Rute
AU - Archer, Margarida
AU - Dubin, Grzegorz
PY - 2020/10
Y1 - 2020/10
N2 - 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.
AB - 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.
KW - IIA subunit
KW - Mannose PTS
KW - Phosphotransferase system
KW - Streptococcus pneumoniae
KW - Sugar transport
KW - X-ray crystallography
UR - http://www.scopus.com/inward/record.url?scp=85092463129&partnerID=8YFLogxK
U2 - 10.3390/molecules25204633
DO - 10.3390/molecules25204633
M3 - Article
C2 - 33053673
AN - SCOPUS:85092463129
VL - 25
JO - Molecules
JF - Molecules
SN - 1420-3049
IS - 20
M1 - 4633
ER -