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• W3015979084 abstract "Abstract The mutated nickase Nt.BspD6I E418A has been obtained by site-directed mutagenesis. The purified protein has been crystallized, and its spatial structure has been determined at 2.45 A resolution. An analysis of the crystal structures of the wild-type and mutated nickase have shown that the elimination of a carboxyl group due to the E418A mutation initiates marked conformational changes in both the N-terminal recognition domain and the C-terminal catalytic domain of nickase and insignificantly affects its linker domain. This is supported by changes in the functional properties of mutated nickase: an increase in the oligomerization capacity in the presence of a substrate, a reduction in the capacity to bind a substrate, and complete loss of catalytic activity." @default.
• W3015979084 created "2020-04-17" @default.
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• W3015979084 date "2020-06-01" @default.
• W3015979084 modified "2023-09-26" @default.
• W3015979084 title "The key role of E418 carboxyl group in the formation of Nt.BspD6I nickase active site: Structural and functional properties of Nt.BspD6I E418A mutant" @default.
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• W3015979084 doi "https://doi.org/10.1016/j.jsb.2020.107508" @default.
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