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==New Delhi Metallo-Beta-Lactamase==
==New Delhi Metallo-Beta-Lactamase==
<Structure load='4eyl' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here NDN1' />
<Structure load='4eyl' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here NDN1' />
The New Delhi metallo-beta-lactamase (<scene name='37/372730/Asymmetrical_4eyl/2'>NMD-)</scene>) in complex with meropenem demonstrates the mechanism in which the active site binds and hydrolyzed the a carbapenem, in this case meropenem.
The New Delhi metallo-beta-lactamase (<scene name='37/372730/Asymmetrical_4eyl/2'>NMD-1</scene>) in complex with meropenem demonstrates the mechanism in which the active site binds and hydrolyzed the a carbapenem, in this case meropenem.
Zn1 (coordinated by three histidine residues), acts as a major constituent of oxyanion hole to stabilize tetrahedral intermediate. It also acts as a Lewis acid for interaction with lactam carbonyl in Michaelis complex and acts to suppress the pKa of the hyrdolytic water to (~5-6) to facilitate it's nucleophilic role.
Zn1 (coordinated by three histidine residues), acts as a major constituent of oxyanion hole to stabilize tetrahedral intermediate. It also acts as a Lewis acid for interaction with lactam carbonyl in Michaelis complex and acts to suppress the pKa of the hyrdolytic water to (~5-6) to facilitate it's nucleophilic role.

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Wayne Decatur, Student, Meng Han Liu, Allison Granberry