6o70

Crystal structure of Csm6 H132A mutant in complex with cA4 by cocrystallization of cA4 and Csm6 H132A mutant

spinqualitylabelsall models 6o70, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6o70 is a 2 chain structure with sequence from Thermococcus onnurineus NA1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: ACK, LQJ Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B6YWC3_THEON Publication Abstract from PubMed Type III-A CRISPR-Cas surveillance complexes containing multi-subunit Csm effector, guide, and target RNAs exhibit multiple activities, including formation of cyclic-oligoadenylates (cAn) from ATP and subsequent cAn-mediated cleavage of single-strand RNA (ssRNA) by the trans-acting Csm6 RNase. Our structure-function studies have focused on Thermococcus onnurineus Csm6 to deduce mechanistic insights into how cA4 binding to the Csm6 CARF domain triggers the RNase activity of the Csm6 HEPN domain and what factors contribute to regulation of RNA cleavage activity. We demonstrate that the Csm6 CARF domain is a ring nuclease, whereby bound cA4 is stepwise cleaved initially to ApApApA>p and subsequently to ApA>p in its CARF domain-binding pocket, with such cleavage bursts using a timer mechanism to regulate the RNase activity of the Csm6 HEPN domain. In addition, we establish T. onnurineus Csm6 as an adenosine-specific RNase and identify a histidine in the cA4 CARF-binding pocket involved in autoinhibitory regulation of RNase activity. CRISPR-Cas III-A Csm6 CARF Domain Is a Ring Nuclease Triggering Stepwise cA4 Cleavage with ApA>p Formation Terminating RNase Activity.,Jia N, Jones R, Yang G, Ouerfelli O, Patel DJ Mol Cell. 2019 Jun 28. pii: S1097-2765(19)30447-2. doi:, 10.1016/j.molcel.2019.06.014. PMID:31326273 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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