View source for 6qnz


==Crystal structure of the site-specific DNA nickase N.BspD6I E418A Mutant==
<StructureSection load='6qnz' size='340' side='right'caption='[[6qnz]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6qnz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._D6 Bacillus sp. D6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QNZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QNZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6qnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qnz OCA], [https://pdbe.org/6qnz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qnz RCSB], [https://www.ebi.ac.uk/pdbsum/6qnz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qnz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A3FEV7_9BACI A3FEV7_9BACI] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:32298813</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6qnz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus sp. D6]]
[[Category: Large Structures]]
[[Category: Artyukh RI]]
[[Category: Atanasov BP]]
[[Category: Fatkhullin BF]]
[[Category: Gabdulkhakov AG]]
[[Category: Kachalova GS]]
[[Category: Perevyazova TA]]
[[Category: Popov AN]]
[[Category: Yunusova AK]]
[[Category: Zheleznaya LA]]