3W2V

Crystal structure of the Cmr2dHD-Cmr3 subcomplex bound to 3'-AMP

Summary for 3W2V

• Entry DOI: 10.2210/pdb3w2v/pdb
• Related: 3W2W
• Descriptor: CRISPR system Cmr subunit Cmr2, CRISPR system Cmr subunit Cmr3, ZINC ION, ... (5 entities in total)
• Functional Keywords: ferredoxin-like fold, immune system
• Biological source: Pyrococcus furiosus; More
• Cellular location: Cytoplasm: Q8U1S6 Q8U1S7
• Total number of polymer chains: 2
• Total formula weight: 115005.39

Authors

Numata, T.,Osawa, T. (deposition date: 2012-12-06, release date: 2013-10-16, Last modification date: 2024-10-30)

Primary citation

Osawa, T.,Inanaga, H.,Numata, T.
Crystal Structure of the Cmr2-Cmr3 Subcomplex in the CRISPR-Cas RNA Silencing Effector Complex.
J.Mol.Biol., 425:3811-3823, 2013

PubMed Abstract: Clustered, regularly interspaced, short palindromic repeat (CRISPR) loci found in prokaryotes are transcribed to produce CRISPR RNAs (crRNAs) that, together with CRISPR-associated (Cas) proteins, target and degrade invading genetic materials. Cmr proteins (Cmr1-6) and crRNA form a sequence-specific RNA silencing effector complex. Here, we report the crystal structures of the Pyrococcus furiosus Cmr2-Cmr3 subcomplex bound with nucleotides (3'-AMP or ATP). The association of Cmr2 and Cmr3 forms an idiosyncratic crevasse, which binds the nucleotides. Cmr3 shares structural similarity with Cas6, which cleaves precursor crRNA for maturation, suggesting the divergent evolution of these proteins. Due to the structural resemblance, the properties of the RNA binding surface observed in Cas6 are well conserved in Cmr3, indicating the RNA binding ability of Cmr3. This surface of Cmr3 constitutes the crevasse observed in the Cmr2-Cmr3 complex. Our findings suggest that the Cmr2-Cmr3 complex uses the crevasse to bind crRNA and/or substrate RNA during the reaction.

PubMed: 23583914
DOI: 10.1016/j.jmb.2013.03.042

Experimental method

X-RAY DIFFRACTION (2.6 Å)