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- W2139458901 abstract "The role of cis−trans isomerizations of peptidyl−proline bonds in the enzyme activity of staphylococcal nuclease (SNase) was examined by mutation of proline residues. The proline-free SNase ([Pro-]SNase), namely, P11A/P31A/P42A/P47T/P56A/P117G-mutant SNase, was adopted for elucidating the correlation between the nuclease activity and the backbone conformational and dynamic states of SNase. The 3D solution structure of [Pro-]SNase has been determined by heteronuclear NMR experiments. Comparing the structure of [Pro-]SNase with the structure of SNase revealed the conformational differences between the two proteins. In the structure of [Pro-]SNase, conformational rearrangements were observed for the loop of residues Ala112−His121 containing a trans Lys116−Gly117 peptide bond and for the C-terminal α-helical loop of residues Leu137−Glu142. Mutation of proline at position 117 also caused the conformational rearrangement of the p-loop (Asp77−Leu89), which is remote from the Ala112−His121 loop. The Ala112−His121 loop and p-loop are placed closer to each other in [Pro-]SNase than in SNase. The backbone dynamic features of the ω-loop (Pro42−Pro56) of SNase are different from those of [Pro-]SNase. The backbone of the ω-loop exhibits restricted flexibility with slow conformational exchange motions in SNase, but is highly flexible in [Pro-]SNase. The analysis indicates that the restrained backbone conformation of the Ala112−His121 loop and restricted flexibility of the ω-loop are two dominant factors determining the enzyme activity of SNase. Of the two factors, the former is correlated with the strained cis Lys116−Pro117 peptide bond and the latter is correlated with the cis−trans isomerizations of the His46−Pro47 peptide bond." @default.
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- W2139458901 date "2007-09-22" @default.
- W2139458901 modified "2023-10-16" @default.
- W2139458901 title "Restricted Backbone Conformational and Motional Flexibilities of Loops Containing Peptidyl−Proline Bonds Dominate the Enzyme Activity of Staphylococcal Nuclease<sup>,</sup>" @default.
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- W2139458901 doi "https://doi.org/10.1021/bi7009794" @default.
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