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- W2004049649 abstract "The three-dimensional structure of the RNA-modifying enzyme, ψ55 tRNA pseudouridine synthase from Mycobacterium tuberculosis, is reported. The 1.9-Å resolution crystal structure reveals the enzyme, free of substrate, in two distinct conformations. The structure depicts an interesting mode of protein flexibility involving a hinged bending in the central β-sheet of the catalytic module. Key parts of the active site cleft are also found to be disordered in the substrate-free form of the enzyme. The hinge bending appears to act as a clamp to position the substrate. Our structural data furthers the previously proposed mechanism of tRNA recognition. The present crystal structure emphasizes the significant role that protein dynamics must play in tRNA recognition, base flipping, and modification. The three-dimensional structure of the RNA-modifying enzyme, ψ55 tRNA pseudouridine synthase from Mycobacterium tuberculosis, is reported. The 1.9-Å resolution crystal structure reveals the enzyme, free of substrate, in two distinct conformations. The structure depicts an interesting mode of protein flexibility involving a hinged bending in the central β-sheet of the catalytic module. Key parts of the active site cleft are also found to be disordered in the substrate-free form of the enzyme. The hinge bending appears to act as a clamp to position the substrate. Our structural data furthers the previously proposed mechanism of tRNA recognition. The present crystal structure emphasizes the significant role that protein dynamics must play in tRNA recognition, base flipping, and modification." @default.
- W2004049649 created "2016-06-24" @default.
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- W2004049649 date "2004-06-01" @default.
- W2004049649 modified "2023-09-29" @default.
- W2004049649 title "Crystal Structure of the Apo Forms of ψ 55 tRNA Pseudouridine Synthase from Mycobacterium tuberculosis" @default.
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- W2004049649 doi "https://doi.org/10.1074/jbc.m401045200" @default.
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