Mathieu, Magali <br/><br/>
Escherichia coli FolC structure reveals an unexpected dihydrofolate binding site providing an attractive target for anti-microbial therapy.  [electronic resource] 

 -  The Journal of biological chemistry  May 2005 
 - 18916-22 p.  digital 
<br/><br/> Publication Type: Journal Article 
<br/><br/><label>ISSN: </label>0021-9258 
<br/><br/><label>Standard No.: </label>10.1074/jbc.M413799200  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Adenosine Triphosphate--chemistry<br/>Anti-Infective Agents--pharmacology<br/>Binding Sites<br/>Catalysis<br/>Catalytic Domain<br/>Crystallography, X-Ray<br/>Escherichia coli--enzymology<br/>Escherichia coli Proteins<br/>Lactobacillus--enzymology<br/>Models, Chemical<br/>Models, Molecular<br/>Multienzyme Complexes--chemistry<br/>Peptide Synthases--chemistry<br/>Protein Binding<br/>Protein Conformation<br/>Protein Structure, Secondary<br/>Pterins--chemistry