Download MendeleySolution structure of the parvulin-type PPIase domain of Staphylococcus aureus PrsA - Implications for the catalytic mechanism of parvulins.
Heikkinen, O., Seppala, R., Tossavainen, H., Heikkinen, S., Koskela, H., Permi, P., Kilpelainen, I.(2009) BMC Struct Biol 9: 17-17
- PubMed: 19309529
- DOI: https://doi.org/10.1186/1472-6807-9-17
- Primary Citation of Related Structures:
2JZV - PubMed Abstract:
Staphylococcus aureus is a Gram-positive pathogenic bacterium causing many kinds of infections from mild respiratory tract infections to life-threatening states as sepsis. Recent emergence of S. aureus strains resistant to numerous antibiotics has created a need for new antimicrobial agents and novel drug targets. S. aureus PrsA is a membrane associated extra-cytoplasmic lipoprotein which contains a parvulin-type peptidyl-prolyl cis-trans isomerase domain. PrsA is known to act as an essential folding factor for secreted proteins in Gram-positive bacteria and thus it is a potential target for antimicrobial drugs against S. aureus.
Organizational Affiliation:
Department of Chemistry, University of Helsinki, Finland. outi.k.heikkinen@helsinki.fi
