Effect of Reversion Back to Cys11 on the Structure and Function of S11C Cys-free Nt.BspD6I

R. I. Artyukh; Артюх Р. И.; B. F. Fatkhullin; Фатхуллин Б. Ф.; V. N. Antipova; Антипова В. Н.; T. A. Perevyazova; Перевязова Т. А.; G. S. Kachalova; Качалова Г. С.; A. K. Yunusova; Юнусова А. К.

doi:10.31857/S0023476123600702

Effect of Reversion Back to Cys11 on the Structure and Function of S11C Cys-free Nt.BspD6I

Authors: Artyukh R.I.¹, Fatkhullin B.F.², Antipova V.N.¹, Perevyazova T.A.¹, Kachalova G.S.¹, Yunusova A.K.¹
Affiliations:
1. Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290, Pushchino, Moscow oblast, Russia
2. Institute of Protein Research, Russian Academy of Sciences, 142290, Pushchino, Moscow oblast, Russia
Issue: Vol 68, No 6 (2023)
Pages: 859-865
Section: STRUCTURE OF MACROMOLECULAR COMPOUNDS
URL: https://rjmseer.com/0023-4761/article/view/673267
DOI: https://doi.org/10.31857/S0023476123600702
EDN: https://elibrary.ru/YEJZJU
ID: 673267

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Abstract

The three-dimensional structure of recombinant nicking endonuclease S11C Cys-free Nt.BspD6I was determined at 1.85 Å resolution. Nickase S11C Cys-free Nt.BspD6I was produced by the reversion back to Cys11 in Cys-free Nt.BspD6I using site-directed mutagenesis. An analysis of the crystal structure of nickase S11C Cys-free Nt.BspD6I demonstrated that the reversion back to Cys11 induces significant conformational changes in the recognition domain of nickase, which are accompanied by changes in its functions, such as a decrease in the affinity to DNA, the loss of the ability to undergo oligomerization, and high activity of restriction endonuclease S11C Cys-free R.BspD6I.

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