Sandbox 122
From Proteopedia
| Line 4: | Line 4: | ||
<Structure load='4eyl' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene NDM1' /> | <Structure load='4eyl' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene NDM1' /> | ||
| + | The NDM-1 is a metallo-protein and associated with the bacterial cell membrane. The active site contains key features for hydrolyzing carbapenems: | ||
| + | - Zinc ion 1(Zn1) is coordinated by three histidine residues: H120, H122 and H189 | ||
| - | + | - Zinc ion (Zn2) is coordinated by three residues: H250, C208 and D124 | |
Revision as of 17:20, 20 July 2016
New Delhi Metallo-Beta-Lactamase
The New Delhi metallo-beta-lactamse in complex with meropenem demonstrates the mechanism in which the active site binds and hydrolyzes the 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. Zn1 also acts to suppress the pka of the hydrolytic water to (~5-6) to facilitate it's nucleophillic role.
|
The NDM-1 is a metallo-protein and associated with the bacterial cell membrane. The active site contains key features for hydrolyzing carbapenems: - Zinc ion 1(Zn1) is coordinated by three histidine residues: H120, H122 and H189
- Zinc ion (Zn2) is coordinated by three residues: H250, C208 and D124
