Fighting Tuberculosis – : Structural Studies of Three Mycobacterial Proteins
作者： Alina Castell
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摘要: A large fraction of the Mycobacterium tuberculosis genome codes for proteins unknown function. We here report structure one these proteins, Rv0130, solved to a resolution 1.8 angstrom. The Rv0130 monomer features single hotdog fold composed highly curved beta-sheet on top long and short alpha-helix. Two monomers in turn pack form double-hotdog-folded homodimer, similar group enzymes that use thiol esters as substrates. was found contain conserved R-specific hydratase motif buried deeply between two monomers. Our biochemical studies show protein is able hydrate trans-2-enoyl-coenzyme moiety with k(cat) 1.1 x 10(2) sec(-1). importance side chains D40 H45 activity demonstrated by site-directed mutagenesis. In contrast many hotdog-folded proline residue distorts central helix Rv0130. This distortion allows creation long, tunnel, substrate-binding channels long-chain eukaryotic 2 enzymes.
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