8v44

N-terminal truncation of CRISPR-associated DinG

spinqualitylabelsall models 8v44, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8v44 is a 1 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0AA82WPF0_PSEAI 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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