NDM-1, the ultimate promiscuous enzyme:
NDM-1 simulation active site. The protein is depicted as a surface and the (imipenem) substrate is colored as in Fig. 1, except for carbon atoms, which are cyan here. A) Substrate recognition is provided by interactions between the zinc ions and the carboxyl and carbonyl oxygen atoms of the substrate (dashed yellow lines) and nonspecific, generally hydrophobic interactions with the protein. The oriented water molecule occupies a pocket between the zinc ions. B) When the mobile loops move, a thin film of water surrounds the substrate, including 2 water molecules that serve as the nucleophile and as the source of the final proton required for ring cleavage (dashed green lines).
Credit: Kim Y, Cunningham MA, Mire J, Tesar C, Sacchettini J, Joachimiak A. NDM-1, the ultimate promiscuous enzyme: substrate recognition and catalytic mechanism. FASEB J. 2013 May;27(5):1917-27.
NDM-1, the ultimate promiscuous enzyme:
NDM-1 simulation active site. The protein is depicted as a surface and the (imipenem) substrate is colored as in Fig. 1, except for carbon atoms, which are cyan here. A) Substrate recognition is provided by interactions between the zinc ions and the carboxyl and carbonyl oxygen atoms of the substrate (dashed yellow lines) and nonspecific, generally hydrophobic interactions with the protein. The oriented water molecule occupies a pocket between the zinc ions. B) When the mobile loops move, a thin film of water surrounds the substrate, including 2 water molecules that serve as the nucleophile and as the source of the final proton required for ring cleavage (dashed green lines).
Credit: Kim Y, Cunningham MA, Mire J, Tesar C, Sacchettini J, Joachimiak A. NDM-1, the ultimate promiscuous enzyme: substrate recognition and catalytic mechanism. FASEB J. 2013 May;27(5):1917-27.