Structural highlights
Function
A3FEV7_9BACI
Publication Abstract from PubMed
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.
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
- ↑ Artyukh RI, Kachalova GS, Yunusova AK, Fatkhullin BF, Atanasov BP, Perevyazova TA, Popov AN, Gabdulkhakov AG, Zheleznaya LA. 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. J Struct Biol. 2020 Apr 13:107508. doi: 10.1016/j.jsb.2020.107508. PMID:32298813 doi:http://dx.doi.org/10.1016/j.jsb.2020.107508
