Penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus

Authors

  • Jennifer Fishovitz,

    1. Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA
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  • Juan A. Hermoso,

    1. Department of Crystallography and Structural Biology, Instituto de Química-Física “Rocasolano,” CSIC, Serrano, Madrid, Spain
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  • Mayland Chang,

    1. Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA
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  • Shahriar Mobashery

    Corresponding author
    1. Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA
    • Address correspondence to: Shahriar Mobashery, Department of Chemistry and Biochemistry, Nieuwland Science Hall, Notre Dame, IN 46556, USA. Tel: 574-631-2933. Fax: 574-631-6652. E-mail: mobashery@nd.edu

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Abstract

High-level resistance to β-lactam antibiotics in methicillin-resistant Staphylococcus aureus (MRSA) is due to expression of penicillin-binding protein 2a (PBP2a), a transpeptidase that catalyzes cell-wall crosslinking in the face of the challenge by β-lactam antibiotics. The activity of this protein is regulated by allostery at a site 60 Å distant from the active site, where crosslinking of cell wall takes place. This review discusses the state of knowledge on this important enzyme of cell-wall biosynthesis in MRSA. © 2014 IUBMB Life, 66(8):572–577, 2014

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