Structural characterization of peptidyl-tRNA hydrolase from Mycobacterium smegmatis by NMR spectroscopy
文摘

NMR solution structure and dynamics of M. smegmatis Pth (MsPth) have been characterized and compared to M. tuberculosis Pth.

MD simulations of MsPth crystal structure indicate flexibility of the lid loop and base loop, while the gate loop is rigid.

MsPth is a stable folded protein with significantly higher stability in comparison to the MtPth.

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