6THH

Crystal structure of type I-D CRISPR-Cas nuclease Cas10d in complex with the SIRV3 AcrID1 (gp02) anti-CRISPR protein

Summary for 6THH

• Entry DOI: 10.2210/pdb6thh/pdb
• Related: 6EXP
• Descriptor: SIRV3 AcrID1 (gp02) anti-CRISPR protein, CRISPR-associated protein, CscA, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: crispr, cas, type i-d, cas10, cas10d, complex, anti-crispr, immune system
• Biological source: Sulfolobus islandicus rudivirus 3; More
• Total number of polymer chains: 3
• Total formula weight: 124665.87

Authors

Manav, M.C.,Brodersen, D.E. (deposition date: 2019-11-20, release date: 2020-10-28, Last modification date: 2024-11-13)

Primary citation

Manav, M.C.,Van, L.B.,Lin, J.,Fuglsang, A.,Peng, X.,Brodersen, D.E.
Structural basis for inhibition of an archaeal CRISPR-Cas type I-D large subunit by an anti-CRISPR protein.
Nat Commun, 11:5993-5993, 2020

PubMed Abstract: 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.

PubMed: 33239638
DOI: 10.1038/s41467-020-19847-x

Experimental method

X-RAY DIFFRACTION (3.48 Å)