Bussiere, D E <br/><br/>
The structure of VanX reveals a novel amino-dipeptidase involved in mediating transposon-based vancomycin resistance.  [electronic resource] 

 -  Molecular cell  Jul 1998 
 - 75-84 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article 
<br/><br/><label>ISSN: </label>1097-2765 
<br/><br/><label>Standard No.: </label>10.1016/s1097-2765(00)80115-x  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Alanine--metabolism<br/>Amino Acid Sequence<br/>Animals<br/>Bacterial Proteins--antagonists & inhibitors<br/>Binding Sites<br/>Carboxypeptidases--chemistry<br/>Copper--pharmacology<br/>Crystallography, X-Ray<br/>DNA Transposable Elements--genetics<br/>Dipeptidases--antagonists & inhibitors<br/>Dipeptides--metabolism<br/>Drug Resistance, Microbial--genetics<br/>Enterococcus faecium--enzymology<br/>Enzyme Inhibitors--pharmacology<br/>Hedgehog Proteins<br/>Mice<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Organophosphorus Compounds--pharmacology<br/>Propionates--pharmacology<br/>Protein Conformation<br/>Proteins--chemistry<br/>Sequence Alignment<br/>Sequence Homology, Amino Acid<br/>Serine-Type D-Ala-D-Ala Carboxypeptidase<br/>Structure-Activity Relationship<br/>Trans-Activators<br/>Vancomycin--pharmacology