Oelschlaeger, Peter <br/><br/>
Hydroxyl groups in the betabeta sandwich of metallo-beta-lactamases favor enzyme activity: Tyr218 and Ser262 pull down the lid.  [electronic resource] 

 -  Journal of molecular biology  Feb 2007 
 - 316-29 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0022-2836 
<br/><br/><label>Standard No.: </label>10.1016/j.jmb.2006.11.027  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Catalysis<br/>Computer Simulation<br/>Enzyme Activation<br/>Hydrogen Bonding<br/>Hydroxides--chemistry<br/>Metals--chemistry<br/>Models, Molecular<br/>Molecular Structure<br/>Mutation<br/>Protein Structure, Tertiary<br/>Serine--chemistry<br/>Structure-Activity Relationship<br/>Tyrosine--chemistry<br/>Zinc--chemistry<br/>beta-Lactamases--chemistry