8V44

N-terminal truncation of CRISPR-associated DinG

Summary for 8V44

• Entry DOI: 10.2210/pdb8v44/pdb
• Descriptor: CasDinG (1 entity in total)
• Functional Keywords: helicase, crispr-associated protein, dna binding protein
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 1
• Total formula weight: 78585.05

Authors

Hallmark, T.,Jackson, R.N. (deposition date: 2023-11-28, release date: 2024-01-17, Last modification date: 2024-07-31)

Primary citation

Hallmark, T.,Williams, A.A.,Redman, O.,Guinn, B.,Judd, C.,Jackson, R.N.
The N-terminal domain of Type IV-A1 CRISPR-associated DinG is vulnerable to proteolysis.
MicroPubl Biol, 2024:-, 2024

PubMed Abstract: 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°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.

PubMed: 38911435
DOI: 10.17912/micropub.biology.001226

Experimental method

X-RAY DIFFRACTION (2.9 Å)