7v01 | pdb_00007v01

Staphylococcus epidermidis RP62a CRISPR short effector complex with self RNA target and ATP

spinqualitylabelsall models 7v01, resolution 3.67Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7v01 is a 10 chain structure with sequence from Staphylococcus epidermidis RP62A. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [Q5HK91_STAEQ] Publication Abstract from PubMed Clustered regularly interspaced short palindromic repeats (CRISPR) and their CRISPR-associated proteins (Cas) provide many prokaryotes with an adaptive immune system against invading genetic material. Type III CRISPR systems are unique in that they can degrade both RNA and DNA. In response to invading nucleic acids, they produce cyclic oligoadenylates that act as secondary messengers, activating cellular nucleases that aid in the immune response. Here, we present seven single-particle cryo-EM structures of the type III-A Staphylococcus epidermidis CRISPR effector complex. The structures reveal the intact S. epidermidis effector complex in an apo, ATP-bound, cognate target RNA-bound, and non-cognate target RNA-bound states and illustrate how the effector complex binds and presents crRNA. The complexes bound to target RNA capture the type III-A effector complex in a post-RNA cleavage state. The ATP-bound structures give details about how ATP binds to Cas10 to facilitate cyclic oligoadenylate production. Structures of an active type III-A CRISPR effector complex.,Smith EM, Ferrell S, Tokars VL, Mondragon A Structure. 2022 Aug 4;30(8):1109-1128.e6. doi: 10.1016/j.str.2022.05.013. Epub, 2022 Jun 16. PMID:35714601 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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