6qnz
From Proteopedia
(Difference between revisions)
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<StructureSection load='6qnz' size='340' side='right'caption='[[6qnz]], [[Resolution|resolution]] 2.45Å' scene=''> | <StructureSection load='6qnz' size='340' side='right'caption='[[6qnz]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[6qnz]] is a 2 chain structure. 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 [http:// | + | <table><tr><td colspan='2'>[[6qnz]] is a 2 chain structure with sequence from [http://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 [http://proteopedia.org/fgij/fg.htm?mol=6QNZ FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </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'>[http:// | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bspD6R1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=127889 Bacillus sp. D6])</td></tr> |
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6qnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qnz OCA], [http://pdbe.org/6qnz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qnz RCSB], [http://www.ebi.ac.uk/pdbsum/6qnz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qnz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | <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®/PubMed®, 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__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Bacillus sp. d6]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Artyukh, R I]] | [[Category: Artyukh, R I]] |
Revision as of 07:03, 29 April 2020
Crystal structure of the site-specific DNA nickase N.BspD6I E418A Mutant
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