4RDP

Crystal structure of Cmr4

4RDP の概要

• エントリーDOI: 10.2210/pdb4rdp/pdb
• 分子名称: CRISPR system Cmr subunit Cmr4 (1 entity in total)
• 機能のキーワード: rrm, rna binding protein, ferredoxin-like fold
• 由来する生物種: Pyrococcus furiosus
• 細胞内の位置: Cytoplasm : Q8U1S9
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67427.30

構造登録者

Shao, Y.,Tang, L.,Li, H. (登録日: 2014-09-19, 公開日: 2014-12-24, 最終更新日: 2024-02-28)

主引用文献

Ramia, N.F.,Spilman, M.,Tang, L.,Shao, Y.,Elmore, J.,Hale, C.,Cocozaki, A.,Bhattacharya, N.,Terns, R.M.,Terns, M.P.,Li, H.,Stagg, S.M.
Essential Structural and Functional Roles of the Cmr4 Subunit in RNA Cleavage by the Cmr CRISPR-Cas Complex.
Cell Rep, 9:1610-1617, 2014

PubMed Abstract: The Cmr complex is the multisubunit effector complex of the type III-B clustered regularly interspaced short palindromic repeats (CRISPR)-Cas immune system. The Cmr complex recognizes a target RNA through base pairing with the integral CRISPR RNA (crRNA) and cleaves the target at multiple regularly spaced locations within the complementary region. To understand the molecular basis of the function of this complex, we have assembled information from electron microscopic and X-ray crystallographic structural studies and mutagenesis of a complete Pyrococcus furiosus Cmr complex. Our findings reveal that four helically packed Cmr4 subunits, which make up the backbone of the Cmr complex, act as a platform to support crRNA binding and target RNA cleavage. Interestingly, we found a hook-like structural feature associated with Cmr4 that is likely the site of target RNA binding and cleavage. Our results also elucidate analogies in the mechanisms of crRNA and target molecule binding by the distinct Cmr type III-A and Cascade type I-E complexes.

PubMed: 25482566
DOI: 10.1016/j.celrep.2014.11.007

実験手法

X-RAY DIFFRACTION (2.85 Å)