4RDP

Crystal structure of Cmr4

Summary for 4RDP

• Entry DOI: 10.2210/pdb4rdp/pdb
• Descriptor: CRISPR system Cmr subunit Cmr4 (1 entity in total)
• Functional Keywords: rrm, rna binding protein, ferredoxin-like fold
• Biological source: Pyrococcus furiosus
• Cellular location: Cytoplasm : Q8U1S9
• Total number of polymer chains: 2
• Total formula weight: 67427.30

Authors

Shao, Y.,Tang, L.,Li, H. (deposition date: 2014-09-19, release date: 2014-12-24, Last modification date: 2024-02-28)

Primary citation

Ramia, N.F.,Spilman, M.,Tang, L.,Shao, Y.,Elmore, J.,Hale, C.,Cocozaki, A.,Bhattacharya, N.,Terns, R.M.,Terns, M.P.,Li, H.,Stagg, S.M.
Essential Structural and Functional Roles of the Cmr4 Subunit in RNA Cleavage by the Cmr CRISPR-Cas Complex.
Cell Rep, 9:1610-1617, 2014

PubMed Abstract: The Cmr complex is the multisubunit effector complex of the type III-B clustered regularly interspaced short palindromic repeats (CRISPR)-Cas immune system. The Cmr complex recognizes a target RNA through base pairing with the integral CRISPR RNA (crRNA) and cleaves the target at multiple regularly spaced locations within the complementary region. To understand the molecular basis of the function of this complex, we have assembled information from electron microscopic and X-ray crystallographic structural studies and mutagenesis of a complete Pyrococcus furiosus Cmr complex. Our findings reveal that four helically packed Cmr4 subunits, which make up the backbone of the Cmr complex, act as a platform to support crRNA binding and target RNA cleavage. Interestingly, we found a hook-like structural feature associated with Cmr4 that is likely the site of target RNA binding and cleavage. Our results also elucidate analogies in the mechanisms of crRNA and target molecule binding by the distinct Cmr type III-A and Cascade type I-E complexes.

PubMed: 25482566
DOI: 10.1016/j.celrep.2014.11.007

Experimental method

X-RAY DIFFRACTION (2.85 Å)