Penicillin binding proteins
（重定向自Penicillin binding protein）
![Ribbon representation of the atomic structure of Penicillin Binding Protein 3 from Pseudomonas aeruginosa (PDB 3OC2),[1] image created with PyMol.](/Images/godic/202502/01/3OC2_Wiki2346.png")
![Penicillin core](/Images/godic/202502/01/Penicillin-core2347.png")
![PBPs normally catalyze the cross-linking of the bacterial cell wall, but they can be permanently inhibited by penicillin and other β-lactam antibiotics. (NAM = N-acetylmuramic acid; NAG = N-acetylglucosamine)](/Images/godic/202502/01/Penicillin_inhibition.svg2347.png")
Penicillin-binding proteins (PBPs) are a group of proteins that are characterized by their affinity for and binding of penicillin. They are a normal constituent of many bacteria; the name just reflects the way by which the protein was discovered. All β-lactam antibiotics (except for tabtoxinine-β-lactam, which inhibits glutamine synthetase) bind to PBPs, which are essential for bacterial cell wall synthesis.