Escherichia coli FolC structure reveals an unexpected dihydrofolate binding site providing an attractive target for anti-microbial therapy. [electronic resource]
Producer: 20050712Description: 18916-22 p. digitalISSN:- 0021-9258
- Adenosine Triphosphate -- chemistry
- Anti-Infective Agents -- pharmacology
- Binding Sites
- Catalysis
- Catalytic Domain
- Crystallography, X-Ray
- Escherichia coli -- enzymology
- Escherichia coli Proteins
- Lactobacillus -- enzymology
- Models, Chemical
- Models, Molecular
- Multienzyme Complexes -- chemistry
- Peptide Synthases -- chemistry
- Protein Binding
- Protein Conformation
- Protein Structure, Secondary
- Pterins -- chemistry
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Publication Type: Journal Article
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