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7UZY

Staphylococcus epidermidis RP62A CRISPR effector complex with non-self target RNA 2

Summary for 7UZY
Entry DOI10.2210/pdb7uzy/pdb
EMDB information26922
DescriptorCRISPR system single-strand-specific deoxyribonuclease Cas10/Csm1 (subtype III-A), CRISPR system Cms protein Csm2, CRISPR system Cms endoribonuclease Csm3, ... (6 entities in total)
Functional Keywordstype iiia crispr, effector complex, rna binding protein, hydrolase-rna complex, hydrolase/rna
Biological sourceStaphylococcus epidermidis RP62A
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Total number of polymer chains11
Total formula weight289284.67
Authors
Smith, E.M.,Ferrell, S.H.,Tokars, V.L.,Mondragon, A. (deposition date: 2022-05-09, release date: 2022-07-06, Last modification date: 2024-10-23)
Primary citationSmith, E.M.,Ferrell, S.,Tokars, V.L.,Mondragon, A.
Structures of an active type III-A CRISPR effector complex.
Structure, 30:1109-1128.e6, 2022
Cited by
PubMed Abstract: 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.
PubMed: 35714601
DOI: 10.1016/j.str.2022.05.013
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.05 Å)
Structure validation

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