4W8X

Crystal Structure of Cmr1 from Pyrococcus furiosus bound to a nucleotide

Summary for 4W8X

• Entry DOI: 10.2210/pdb4w8x/pdb
• Descriptor: CRISPR system Cmr subunit Cmr1-1, PHOSPHATE ION, GUANOSINE-3'-MONOPHOSPHATE, ... (4 entities in total)
• Functional Keywords: cmr1, cmr complex, nucleotide-bound, crispr, rna binding protein
• Biological source: Pyrococcus furiosus
• Cellular location: Cytoplasm : Q8U1S5
• Total number of polymer chains: 1
• Total formula weight: 40240.90

Authors

Benda, C.,Ebert, J.,Baumgaertner, M.,Conti, E. (deposition date: 2014-08-26, release date: 2014-10-15, Last modification date: 2024-01-10)

Primary citation

Benda, C.,Ebert, J.,Scheltema, R.A.,Schiller, H.B.,Baumgartner, M.,Bonneau, F.,Mann, M.,Conti, E.
Structural Model of a CRISPR RNA-Silencing Complex Reveals the RNA-Target Cleavage Activity in Cmr4.
Mol.Cell, 56:43-54, 2014

PubMed Abstract: The Cmr complex is an RNA-guided endonuclease that cleaves foreign RNA targets as part of the CRISPR prokaryotic defense system. We investigated the molecular architecture of the P. furiosus Cmr complex using an integrative structural biology approach. We determined crystal structures of P. furiosus Cmr1, Cmr2, Cmr4, and Cmr6 and combined them with known structural information to interpret the cryo-EM map of the complex. To support structure determination, we obtained residue-specific interaction data using protein crosslinking and mass spectrometry. The resulting pseudoatomic model reveals how the superhelical backbone of the complex is defined by the polymerizing principles of Cmr4 and Cmr5 and how it is capped at the extremities by proteins of similar folds. The inner surface of the superhelix exposes conserved residues of Cmr4 that we show are required for target-cleavage activity. The structural and biochemical data thus identify Cmr4 as the conserved endoribonuclease of the Cmr complex.

PubMed: 25280103
DOI: 10.1016/j.molcel.2014.09.002

Experimental method

X-RAY DIFFRACTION (3 Å)