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Crystal structures of Staphylococcus aureus penicillin binding protein 2a (PBP2a)

In vitro studies identified an allosteric site on PBP2a that could aid the development of new antibiotics to treat methicillin-resistant S. aureus (MRSA) infection. b-Lactam antibiotics inhibit the transpeptidase activity of PBPs; however, MRSA PBP2a is resistant to this inhibition. In vitro, structural studies of PBP2a revealed an allosteric pocket 60 Å away from the transpeptidase active site. Ligand binding to the allosteric site caused a conformational change in PBP2a, exposing the active site for subsequent inhibition by b-lactam antibiotics. Next steps could include looking for compounds that bind to the PBP2a allosteric site.

SciBX 6(41); doi:10.1038/scibx.2013.1172
Published online Oct. 24, 2013

Patent and licensing status undisclosed

Otero, L.H. et al. Proc. Natl. Acad. Sci. USA; published online Oct. 1, 2013;
doi:10.1073/pnas.1300118110
Contact: Juan A. Hermoso, Spanish National Research Council, Madrid, Spain
e-mail:
xjuan@iqfr.csic.es

Contact: Shahriar Mobashery, University of Notre Dame, Notre Dame, Ind.
e-mail:
mobashery@nd.edu