Role of methionine 71 in substrate recognition and structural integrity of bacterial peptidyl-tRNA hydrolase

Conclusion Our results indicate that the interactions of M71 with N14 and H24 play an important role in optimal positioning of their side-chains relative to the peptidyl-tRNA substrate. Overall, these interactions of M71 are important for the activity, stability, and compactness of the protein. Significance The work presented provides original and new structural and dynamics information that significantly enhances our understanding of the network of interactions that govern this enzyme's activity and selectivity.

Source: Biochimica et Biophysica Acta (BBA) Proteins and Proteomics - May 5, 2018 Category: Biochemistry Source Type: research