6yes: Difference between revisions

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'''Unreleased structure'''


The entry 6yes is ON HOLD
==Crystal structure of type I-D CRISPR-Cas nuclease Cas10d==
<StructureSection load='6yes' size='340' side='right'caption='[[6yes]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6yes]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_islandicus_LAL14/1 Sulfolobus islandicus LAL14/1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YES 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]] 4.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6yes FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yes OCA], [https://pdbe.org/6yes PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yes RCSB], [https://www.ebi.ac.uk/pdbsum/6yes PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yes ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/M9U4Y8_SULIS M9U4Y8_SULIS]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A hallmark of type I CRISPR-Cas systems is the presence of Cas3, which contains both the nuclease and helicase activities required for DNA cleavage during interference. In subtype I-D systems, however, the histidine-aspartate (HD) nuclease domain is encoded as part of a Cas10-like large effector complex subunit and the helicase activity in a separate Cas3' subunit, but the functional and mechanistic consequences of this organisation are not currently understood. Here we show that the Sulfolobus islandicus type I-D Cas10d large subunit exhibits an unusual domain architecture consisting of a Cas3-like HD nuclease domain fused to a degenerate polymerase fold and a C-terminal domain structurally similar to Cas11. Crystal structures of Cas10d both in isolation and bound to S. islandicus rod-shaped virus 3 AcrID1 reveal that the anti-CRISPR protein sequesters the large subunit in a non-functional state unable to form a cleavage-competent effector complex. The architecture of Cas10d suggests that the type I-D effector complex is similar to those found in type III CRISPR-Cas systems and that this feature is specifically exploited by phages for anti-CRISPR defence.


Authors:  
Structural basis for inhibition of an archaeal CRISPR-Cas type I-D large subunit by an anti-CRISPR protein.,Manav MC, Van LB, Lin J, Fuglsang A, Peng X, Brodersen DE Nat Commun. 2020 Nov 25;11(1):5993. doi: 10.1038/s41467-020-19847-x. PMID:33239638<ref>PMID:33239638</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6yes" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sulfolobus islandicus LAL14/1]]
[[Category: Brodersen DE]]
[[Category: Manav MC]]
[[Category: Van LB]]

Latest revision as of 13:25, 24 January 2024

Crystal structure of type I-D CRISPR-Cas nuclease Cas10d

6yes, resolution 4.10Å

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