Abstract |
The Mycobacterium tuberculosis rmlC gene encodes dTDP-4-keto-6-deoxyglucose epimerase, the third enzyme in the M. tuberculosis dTDP-L-rhamnose pathway which is essential for mycobacterial cell-wall synthesis. Because it is structurally unique, highly substrate-specific and does not require a cofactor, RmlC is considered to be the most promising drug target in the pathway, and the M. tuberculosis rmlC gene was selected in the initial round of TB Structural Genomics Consortium targets for structure determination. The 1.7 A native structure determined by the consortium facilities is reported and implications for in silico screening of ligands for structure-guided drug design are discussed.
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Authors | Katherine A Kantardjieff, Chang Yub Kim, Cleo Naranjo, Geoffry S Waldo, Timothy Lekin, Brent W Segelke, Adam Zemla, Min S Park, Thomas C Terwilliger, Bernhard Rupp |
Journal | Acta crystallographica. Section D, Biological crystallography
(Acta Crystallogr D Biol Crystallogr)
Vol. 60
Issue Pt 5
Pg. 895-902
(May 2004)
ISSN: 0907-4449 [Print] United States |
PMID | 15103135
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S., Research Support, U.S. Gov't, P.H.S.)
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Chemical References |
- Carbohydrate Epimerases
- dTDP-4-ketorhamnose 3,5-epimerase
- Rhamnose
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Topics |
- Amino Acid Sequence
- Binding Sites
- Carbohydrate Epimerases
(chemistry, metabolism)
- Crystallography, X-Ray
- Dimerization
- Drug Design
- Genomics
- International Cooperation
- Models, Molecular
- Molecular Sequence Data
- Mycobacterium tuberculosis
(enzymology, metabolism)
- Pilot Projects
- Protein Conformation
- Rhamnose
(metabolism)
- Sequence Homology, Amino Acid
- Structural Homology, Protein
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