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

• Published in: IUBMB life 2014-08, Vol.66 (8), p.572-577
• Main Authors: Fishovitz, Jennifer, Hermoso, Juan A., Chang, Mayland, Mobashery, Shahriar
• Format: Article
• Language: English
• Subjects: allosteric regulation; Allosteric Regulation - physiology; beta-Lactams - metabolism; Carbapenems - chemistry; Cell Wall - metabolism; Cephalosporins - chemistry; conformational change; Cross-Linking Reagents - metabolism; Drug Resistance, Bacterial - genetics; Methicillin-Resistant Staphylococcus aureus - genetics; Methicillin-Resistant Staphylococcus aureus - metabolism; methicillin‐resistant Staphylococcus aureus; Models, Molecular; Molecular Structure; Penicillin-Binding Proteins - chemistry; Penicillin-Binding Proteins - genetics; Penicillin-Binding Proteins - metabolism; Penicillins - chemistry; Peptide Synthases - chemistry; Peptide Synthases - genetics; Peptide Synthases - metabolism; resistance mechanism; Staphylococcus aureus; β‐lactam antibiotics
• ISSN: 1521-6543; 1521-6551
• DOI: 10.1002/iub.1289

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