4H4K

Structure of the Cmr2-Cmr3 subcomplex of the Cmr RNA-silencing complex

4H4K の概要

• エントリーDOI: 10.2210/pdb4h4k/pdb
• 分子名称: CRISPR system Cmr subunit Cmr3, CRISPR system Cmr subunit Cmr2, ADENOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: ferredoxin, palm, ramp, repeat associated mysterious protein, polymerase, nuclease, rna-interference, cmr proteins crispr rna, rna binding protein
• 由来する生物種: Pyrococcus furiosus; 詳細
• 細胞内の位置: Cytoplasm : Q8U1S7 Q8U1S6
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 117446.78

構造登録者

Shao, Y.,Cocozaki, A.I.,Ramia, N.F.,Terns, R.M.,Terns, M.P.,Li, H. (登録日: 2012-09-17, 公開日: 2013-03-06, 最終更新日: 2024-02-28)

主引用文献

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

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: 23395183
DOI: 10.1016/j.str.2013.01.002

実験手法

X-RAY DIFFRACTION (2.804 Å)