Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structures of the Cmr-β Complex Reveal the Regulation of the Immunity Mechanism of Type III-B CRISPR-Cas.
Journal, issue, pages	Mol Cell, Vol. 79, Issue 5, Page 741-757.e7, Year 2020
Publish date	Sep 3, 2020
Authors	Nicholas Sofos / Mingxia Feng / Stefano Stella / Tillmann Pape / Anders Fuglsang / Jinzhong Lin / Qihong Huang / Yingjun Li / Qunxin She / Guillermo Montoya /
PubMed Abstract	Cmr-β is a type III-B CRISPR-Cas complex that, upon target RNA recognition, unleashes a multifaceted immune response against invading genetic elements, including single-stranded DNA (ssDNA) ...Cmr-β is a type III-B CRISPR-Cas complex that, upon target RNA recognition, unleashes a multifaceted immune response against invading genetic elements, including single-stranded DNA (ssDNA) cleavage, cyclic oligoadenylate synthesis, and also a unique UA-specific single-stranded RNA (ssRNA) hydrolysis by the Cmr2 subunit. Here, we present the structure-function relationship of Cmr-β, unveiling how binding of the target RNA regulates the Cmr2 activities. Cryoelectron microscopy (cryo-EM) analysis revealed the unique subunit architecture of Cmr-β and captured the complex in different conformational stages of the immune response, including the non-cognate and cognate target-RNA-bound complexes. The binding of the target RNA induces a conformational change of Cmr2, which together with the complementation between the 5' tag in the CRISPR RNAs (crRNA) and the 3' antitag of the target RNA activate different configurations in a unique loop of the Cmr3 subunit, which acts as an allosteric sensor signaling the self- versus non-self-recognition. These findings highlight the diverse defense strategies of type III complexes.
External links	Mol Cell / PubMed:32730741
Methods	EM (single particle)
Resolution	2.41 - 3.52 Å
Structure data	10102 6s6b EMDB-10102, PDB-6s6b: Type III-B Cmr-beta Cryo-EM structure of the Apo state Method: EM (single particle) / Resolution: 2.75 Å 10117 6s8b EMDB-10117, PDB-6s8b: Cryo-EM structure of the Type III-B Cmr-beta bound to cognate target RNA and AMPPnP, state 1 Method: EM (single particle) / Resolution: 2.41 Å 10119 6s8e EMDB-10119, PDB-6s8e: Cryo-EM structure of the type III-B Cmr-beta complex bound to non-cognate target RNA Method: EM (single particle) / Resolution: 3.1 Å 10126 6s91 EMDB-10126, PDB-6s91: Cryo-EM structure of the Type III-B Cmr-beta bound to cognate target RNA and AMPPnP, state 2 Method: EM (single particle) / Resolution: 2.68 Å 10196 6sh8 EMDB-10196, PDB-6sh8: Cryo-EM structure of the Type III-B Cmr-beta bound to cognate target RNA and AMPPnP, state 2, in the presence of ssDNA Method: EM (single particle) / Resolution: 3.14 Å 10197 6shb EMDB-10197, PDB-6shb: Cryo-EM structure of the Type III-B Cmr-beta bound to cognate target RNA and AMPPnP, state 1, in the presence of ssDNA Method: EM (single particle) / Resolution: 3.07 Å 10209 6sic EMDB-10209, PDB-6sic: Cryo-EM structure of the Type III-B Cmr-beta bound to cognate target RNA Method: EM (single particle) / Resolution: 3.52 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-ANP: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogueYM ChemComp-MN*: Unknown entry
Source	sulfolobus islandicus rey15a (acidophilic) sulfolobus islandicus (strain rey15a) (acidophilic) synthetic construct (others)
Keywords	ANTIVIRAL PROTEIN / CRISPR-Cas / Effector complex / nuclease / cyclic oligo-adenylate synthase