title: Same same but different: new structural insight into CRISPR-Cas complexes.
abstract: Three papers in this issue of Molecular Cell report on the structure and functional activity of type III CRISPR-Cas effector complexes, revealing novel and conserved features of the ribonucleoprotein particles that underlie prokaryotic genome defense. The new structures suggest that type I and type III complexes follow the same architectural principles and are most likely descendants of a common ancestor, the differences in RNA and protein sequences and structure of individual components notwithstanding.
authors.affiliation: Institute for Molecular Infection Biology, University of Würzburg, Josef-Schneider-Straße 2, 97080 Würzburg, Germany.
authors.forename: Nadja
authors.initials: N
authors.lastname: Heidrich
authors.forename: Jörg
authors.initials: J
authors.lastname: Vogel
mesh_terms: D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D064130:CRISPR-Associated Proteins / Q000737:chemistry* / Q000378:metabolism*; D020027:Pyrococcus furiosus / Q000378:metabolism*; D034622:RNA Interference; D019642:RNA, Archaeal / Q000378:metabolism*; D012329:RNA, Bacterial / Q000378:metabolism*; D012260:Ribonucleases / Q000378:metabolism*; D048229:Sulfolobus solfataricus / Q000378:metabolism*; D016963:Thermus thermophilus / Q000378:metabolism*
chemical_list: D019843:Archaeal Proteins; D001426:Bacterial Proteins; D064130:CRISPR-Associated Proteins; D019642:RNA, Archaeal; D012329:RNA, Bacterial; D012260:Ribonucleases