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Mycobacterium tuberculosis RmIC epimerase (Rv3465): a promising drug-target structure in the rhamnose pathway

Acta Cryst. (2004). D60, 895–902 [doi:10.1107/S0907444904005323]

[epimerase Rv3465]The 1.7 Å native structure of Mycobacterium tuberculosis rmlC (PDB entry 1UPI) has been recently reported by the TB Structural Genomics Consortium, and implications for virtual ligand screening are discussed. Rhamnose synthetic enzymes have been of particular interest in the development of novel antimycobacterial therapeutics, because L-rhamnose, a sugar not present in the human host, plays a key role as a structural link between the mycobacterial cell-wall components arabinogalactan and peptidoglycan. dTDP-4-keto-6-deoxyglucose epimerase (rmlC), the third enzyme in the dTDP-L-rhamnose pathway, is considered to be the most promising target in the pathway for structure-guided drug design, because rmlC is structurally unique, highly substrate specific, and does not require a cofactor.

K. A. Kantardjieff, C.-Y. Kim, C. Naranjo, G. S. Waldo, T. Lekin, B. W. Segelke, A. Zemla, M. S. Park, T. C. Terwilliger and B. Rupp