View source for 8v44


==N-terminal truncation of CRISPR-associated DinG==
<StructureSection load='8v44' size='340' side='right'caption='[[8v44]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8v44]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8V44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8V44 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]] 2.9&#8491;</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=8v44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8v44 OCA], [https://pdbe.org/8v44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8v44 RCSB], [https://www.ebi.ac.uk/pdbsum/8v44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8v44 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0AA82WPF0_PSEAI A0AA82WPF0_PSEAI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CasDinG is an ATP-dependent 5'-3' DNA helicase essential for bacterial Type IV-A1 CRISPR associated immunity. CasDinG contains an essential N-terminal domain predicted to bind DNA. To better understand the role of the N-terminal domain, we attempted to co-crystallize CasDinG with DNA substrates. We successfully crystallized CasDinG in a tightly packed, crystal conformation with previously unobserved unit cell dimensions. However, the structure lacked electron density for a bound DNA substrate and the CasDinG N-terminal domain. Additionally, the tight crystal packing disallowed space for the N-terminal domain, indicating that the N-terminal domain was proteolyzed before crystallization. Follow up experiments revealed that the N-terminal domain of CasDinG is proteolyzed after a few days at room temperature, but is protected from proteolysis at 4 degrees C. These data provide a distinct x-ray crystal structure of CasDinG and indicate the essential N-terminal domain of CasDinG is prone to proteolysis.

The N-terminal domain of Type IV-A1 CRISPR-associated DinG is vulnerable to proteolysis.,Hallmark T, Williams AA, Redman O, Guinn B, Judd C, Jackson RN MicroPubl Biol. 2024 Jun 5;2024:10.17912/micropub.biology.001226. doi: , 10.17912/micropub.biology.001226. eCollection 2024. PMID:38911435<ref>PMID:38911435</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8v44" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Hallmark T]]
[[Category: Jackson RN]]