4H4K
Structure of the Cmr2-Cmr3 subcomplex of the Cmr RNA-silencing complex
Summary for 4H4K
| Entry DOI | 10.2210/pdb4h4k/pdb |
| Descriptor | CRISPR system Cmr subunit Cmr3, CRISPR system Cmr subunit Cmr2, ADENOSINE-5'-TRIPHOSPHATE, ... (6 entities in total) |
| Functional Keywords | ferredoxin, palm, ramp, repeat associated mysterious protein, polymerase, nuclease, rna-interference, cmr proteins crispr rna, rna binding protein |
| Biological source | Pyrococcus furiosus More |
| Cellular location | Cytoplasm : Q8U1S7 Q8U1S6 |
| Total number of polymer chains | 2 |
| Total formula weight | 117446.78 |
| Authors | Shao, Y.,Cocozaki, A.I.,Ramia, N.F.,Terns, R.M.,Terns, M.P.,Li, H. (deposition date: 2012-09-17, release date: 2013-03-06, Last modification date: 2024-02-28) |
| Primary citation | Shao, Y.,Cocozaki, A.I.,Ramia, N.F.,Terns, R.M.,Terns, M.P.,Li, H. Structure of the cmr2-cmr3 subcomplex of the cmr RNA silencing complex. Structure, 21:376-384, 2013 Cited by PubMed Abstract: 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 (Cas10) and Cmr3 subunits at 2.8 Å 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. PubMed: 23395183DOI: 10.1016/j.str.2013.01.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.804 Å) |
Structure validation
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