4l0k: Difference between revisions
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<StructureSection load='4l0k' size='340' side='right'caption='[[4l0k]], [[Resolution|resolution]] 2.33Å' scene=''> | <StructureSection load='4l0k' size='340' side='right'caption='[[4l0k]], [[Resolution|resolution]] 2.33Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4l0k]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4l0k]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiophilus Deinococcus radiophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L0K FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.328Å</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=4l0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l0k OCA], [https://pdbe.org/4l0k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l0k RCSB], [https://www.ebi.ac.uk/pdbsum/4l0k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l0k ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A067XG67_9DEIO A0A067XG67_9DEIO] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 4l0k" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4l0k" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Endonuclease 3D structures|Endonuclease 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Deinococcus radiophilus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ge | [[Category: Ge J]] | ||
[[Category: Yang | [[Category: Yang M]] | ||
[[Category: Zhuo | [[Category: Zhuo W]] | ||
Latest revision as of 06:10, 21 November 2024
Crystal structure of a type II restriction endonucleaseCrystal structure of a type II restriction endonuclease
Structural highlights
FunctionPublication Abstract from PubMedDraIII is a type IIP restriction endonucleases (REases) that recognizes and creates a double strand break within the gapped palindromic sequence CAC upward arrowNNN downward arrowGTG of double-stranded DNA ( upward arrow indicates nicking on the bottom strand; downward arrow indicates nicking on the top strand). However, wild type DraIII shows significant star activity. In this study, it was found that the prominent star site is CAT upward arrowGTT downward arrowGTG, consisting of a star 5' half (CAT) and a canonical 3' half (GTG). DraIII nicks the 3' canonical half site at a faster rate than the 5' star half site, in contrast to the similar rate with the canonical full site. The crystal structure of the DraIII protein was solved. It indicated, as supported by mutagenesis, that DraIII possesses a betabetaalpha-metal HNH active site. The structure revealed extensive intra-molecular interactions between the N-terminal domain and the C-terminal domain containing the HNH active site. Disruptions of these interactions through site-directed mutagenesis drastically increased cleavage fidelity. The understanding of fidelity mechanisms will enable generation of high fidelity REases. Elimination of inter-domain interactions increases the cleavage fidelity of the restriction endonuclease DraIII.,Zhuo W, Lai X, Zhang L, Chan SH, Li F, Zhu Z, Yang M, Sun D Protein Cell. 2014 May;5(5):357-68. doi: 10.1007/s13238-014-0038-z. Epub 2014 Apr, 15. PMID:24733184[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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