6NE0

Structure of double-stranded target DNA engaged Csy complex from Pseudomonas aeruginosa (PA-14)

Replaces:  6MPU

Summary for 6NE0

• Entry DOI: 10.2210/pdb6ne0/pdb
• EMDB information: 9191
• Descriptor: CRISPR-associated protein Csy1, CRISPR-associated protein Csy2, CRISPR-associated protein Csy3, ... (7 entities in total)
• Functional Keywords: type i-f crispr rna-guided surveillance complex, viral protein mimic, csy-complex, immune system-rna complex, immune system/rna
• Biological source: Pseudomonas aeruginosa UCBPP-PA14; More
• Total number of polymer chains: 12
• Total formula weight: 375916.48

Authors

Chowdhury, S.,Rollins, M.F.,Carter, J.,Golden, S.M.,Miettinen, H.M.,Santiago-Frangos, A.,Faith, D.,Lawrence, M.C.,Wiedenheft, B.,Lander, G.C. (deposition date: 2018-12-15, release date: 2018-12-26, Last modification date: 2024-03-13)

Primary citation

Rollins, M.F.,Chowdhury, S.,Carter, J.,Golden, S.M.,Miettinen, H.M.,Santiago-Frangos, A.,Faith, D.,Lawrence, C.M.,Lander, G.C.,Wiedenheft, B.
Structure Reveals a Mechanism of CRISPR-RNA-Guided Nuclease Recruitment and Anti-CRISPR Viral Mimicry.
Mol. Cell, 74:132-142.e5, 2019

PubMed Abstract: Bacteria and archaea have evolved sophisticated adaptive immune systems that rely on CRISPR RNA (crRNA)-guided detection and nuclease-mediated elimination of invading nucleic acids. Here, we present the cryo-electron microscopy (cryo-EM) structure of the type I-F crRNA-guided surveillance complex (Csy complex) from Pseudomonas aeruginosa bound to a double-stranded DNA target. Comparison of this structure to previously determined structures of this complex reveals a ∼180-degree rotation of the C-terminal helical bundle on the "large" Cas8f subunit. We show that the double-stranded DNA (dsDNA)-induced conformational change in Cas8f exposes a Cas2/3 "nuclease recruitment helix" that is structurally homologous to a virally encoded anti-CRISPR protein (AcrIF3). Structural homology between Cas8f and AcrIF3 suggests that AcrIF3 is a mimic of the Cas8f nuclease recruitment helix.

PubMed: 30872121
DOI: 10.1016/j.molcel.2019.02.001

Experimental method

ELECTRON MICROSCOPY (3.4 Å)