6qnz | pdb_00006qnz
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Crystal structure of the site-specific DNA nickase N.BspD6I E418A Mutant
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Structural highlights
FunctionPublication Abstract from PubMedThe 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. 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.,Artyukh RI, Kachalova GS, Yunusova AK, Fatkhullin BF, Atanasov BP, Perevyazova TA, Popov AN, Gabdulkhakov AG, Zheleznaya LA J Struct Biol. 2020 Apr 13:107508. doi: 10.1016/j.jsb.2020.107508. PMID:32298813[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 12:04, 24 January 2024.