Journal
STRUCTURE
Volume 21, Issue 3, Pages 376-384Publisher
CELL PRESS
DOI: 10.1016/j.str.2013.01.002
Keywords
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Funding
- National Institutes of Health [R01GM0099604, R01GM54682]
- American Heart Association predoctoral fellowship [11PRE7090000]
- United States Department of Energy Office of Science, Office of Basic Energy Sciences [W-31-109-Eng-38]
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The Cmr complex is an RNA-guided effector complex that cleaves invader RNA in the prokaryotic immune response mediated by the CRISPR (Clustered Regularly Interspaced Short Palindromic Repeat)-Cas system. Here, we report the crystal structure of a Cmr subcomplex containing Cmr2 (Cas1 0) and Cmr3 subunits at 2.8 angstrom resolution. The structure revealed a dual ferredoxin fold and glycine-rich loops characteristic of previously known repeat-associated mysterious proteins and two unique insertion elements in Cmr3 that mediate its interaction with Cmr2. Surprisingly, while mutation of both insertion elements significantly weakened Cmr3-Cmr2 interaction, they exhibit differential effects on Cmr-mediated RNA cleavage by the Cmr complex, suggesting stabilization of Cmr2-Cmr3 interactions by other subunits. Further mutational analysis of the two conserved (but non-Cmr2-binding) glycine-rich loops of Cmr3 identified a region that is likely involved in assembly or the RNA cleavage function of the Cmr complex.
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