Green Victoria L, Verma Anil, Owens Raymond J, Phillips Simon E V, Carr Stephen B
Research Complex at Harwell, Rutherford Appleton Laboratory, Harwell Oxford, Didcot, Oxon OX11 0FA, England.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Oct 1;67(Pt 10):1160-4. doi: 10.1107/S1744309111029654. Epub 2011 Sep 6.
Antibiotic resistance in bacterial pathogens poses a serious threat to human health and the metallo-β-lactamase (MBL) enzymes are responsible for much of this resistance. The recently identified New Delhi MBL 1 (NDM-1) is a novel member of this family that is capable of hydrolysing a wide variety of clinically important antibiotics. Here, the crystal structure of NDM-1 from Klebsiella pneumoniae is reported and its structure and active site are discussed in the context of other recently deposited coordinates of NDM-1.
细菌病原体中的抗生素耐药性对人类健康构成严重威胁,金属β-内酰胺酶(MBL)酶在很大程度上导致了这种耐药性。最近发现的新德里金属β-内酰胺酶1(NDM-1)是该家族的一个新成员,能够水解多种临床上重要的抗生素。本文报道了肺炎克雷伯菌中NDM-1的晶体结构,并结合最近存入的其他NDM-1坐标讨论了其结构和活性位点。