7UZZ

Staphylococcus epidermidis RP62a CRISPR tall effector complex

Summary for 7UZZ

• Entry DOI: 10.2210/pdb7uzz/pdb
• EMDB information: 26923
• Descriptor: RNA (37-MER), CRISPR system Cms protein Csm2, CRISPR system Cms protein Csm5, ... (6 entities in total)
• Functional Keywords: type iiia crispr, effector complex, rna binding protein, hydrolase-rna complex, hydrolase/rna
• Biological source: Staphylococcus epidermidis RP62A; More
• Total number of polymer chains: 11
• Total formula weight: 316028.29

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: 2022-08-17)

Primary citation

Smith, 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

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

Experimental method

ELECTRON MICROSCOPY (4.45 Å)