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-Structure paper
| タイトル | Structure and activity of the RNA-targeting Type III-B CRISPR-Cas complex of Thermus thermophilus. |
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| ジャーナル・号・ページ | Mol Cell, Vol. 52, Issue 1, Page 135-145, Year 2013 |
| 掲載日 | 2013年10月10日 |
著者 | Raymond H J Staals / Yoshihiro Agari / Saori Maki-Yonekura / Yifan Zhu / David W Taylor / Esther van Duijn / Arjan Barendregt / Marnix Vlot / Jasper J Koehorst / Keiko Sakamoto / Akiko Masuda / Naoshi Dohmae / Peter J Schaap / Jennifer A Doudna / Albert J R Heck / Koji Yonekura / John van der Oost / Akeo Shinkai / ![]() |
| PubMed 要旨 | The CRISPR-Cas system is a prokaryotic host defense system against genetic elements. The Type III-B CRISPR-Cas system of the bacterium Thermus thermophilus, the TtCmr complex, is composed of six ...The CRISPR-Cas system is a prokaryotic host defense system against genetic elements. The Type III-B CRISPR-Cas system of the bacterium Thermus thermophilus, the TtCmr complex, is composed of six different protein subunits (Cmr1-6) and one crRNA with a stoichiometry of Cmr112131445361:crRNA1. The TtCmr complex copurifies with crRNA species of 40 and 46 nt, originating from a distinct subset of CRISPR loci and spacers. The TtCmr complex cleaves the target RNA at multiple sites with 6 nt intervals via a 5' ruler mechanism. Electron microscopy revealed that the structure of TtCmr resembles a "sea worm" and is composed of a Cmr2-3 heterodimer "tail," a helical backbone of Cmr4 subunits capped by Cmr5 subunits, and a curled "head" containing Cmr1 and Cmr6. Despite having a backbone of only four Cmr4 subunits and being both longer and narrower, the overall architecture of TtCmr resembles that of Type I Cascade complexes. |
リンク | Mol Cell / PubMed:24119403 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 22.0 - 26.0 Å |
| 構造データ | ![]() EMDB-2418: ![]() EMDB-5719: |
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Thermus thermophilus (バクテリア)