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TitleStructure and activity of the RNA-targeting Type III-B CRISPR-Cas complex of Thermus thermophilus.
Journal, issue, pagesMol Cell, Vol. 52, Issue 1, Page 135-145, Year 2013
Publish dateOct 10, 2013
AuthorsRaymond 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 AbstractThe 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.
External linksMol Cell / PubMed:24119403 / PubMed Central
MethodsEM (single particle)
Resolution22.0 - 26.0 Å
Structure data

EMDB-2418:
Structure and activity of an RNA-targeting Type III-B CRISPER-Cas complex
Method: EM (single particle) / Resolution: 22.0 Å

EMDB-5719:
Electron microscopy of the negatively-stained Cmr complex from Thermus thermophilus HB8.
Method: EM (single particle) / Resolution: 26.0 Å

Source
  • Thermus thermophilus (bacteria)

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