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6B45

Cryo-EM structure of Type I-F CRISPR crRNA-guided Csy surveillance complex

Summary for 6B45
Entry DOI10.2210/pdb6b45/pdb
EMDB information7049
DescriptorCRISPR-associated protein Csy1, CRISPR-associated protein Csy2, CRISPR-associated protein Csy3, ... (5 entities in total)
Functional Keywordscrispr-cas, immune system - rna complex, immune system / rna
Biological sourcePseudomonas aeruginosa (strain UCBPP-PA14)
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Total number of polymer chains10
Total formula weight353369.11
Authors
Guo, T.W.,Bartesaghi, A.,Yang, H.,Falconieri, V.,Rao, P.,Merk, A.,Fox, T.,Earl, L.,Patel, D.J.,Subramaniam, S. (deposition date: 2017-09-25, release date: 2017-10-18, Last modification date: 2024-03-13)
Primary citationGuo, T.W.,Bartesaghi, A.,Yang, H.,Falconieri, V.,Rao, P.,Merk, A.,Eng, E.T.,Raczkowski, A.M.,Fox, T.,Earl, L.A.,Patel, D.J.,Subramaniam, S.
Cryo-EM Structures Reveal Mechanism and Inhibition of DNA Targeting by a CRISPR-Cas Surveillance Complex.
Cell, 171:414-426.e12, 2017
Cited by
PubMed Abstract: Prokaryotic cells possess CRISPR-mediated adaptive immune systems that protect them from foreign genetic elements, such as invading viruses. A central element of this immune system is an RNA-guided surveillance complex capable of targeting non-self DNA or RNA for degradation in a sequence- and site-specific manner analogous to RNA interference. Although the complexes display considerable diversity in their composition and architecture, many basic mechanisms underlying target recognition and cleavage are highly conserved. Using cryoelectron microscopy (cryo-EM), we show that the binding of target double-stranded DNA (dsDNA) to a type I-F CRISPR system yersinia (Csy) surveillance complex leads to large quaternary and tertiary structural changes in the complex that are likely necessary in the pathway leading to target dsDNA degradation by a trans-acting helicase-nuclease. Comparison of the structure of the surveillance complex before and after dsDNA binding, or in complex with three virally encoded anti-CRISPR suppressors that inhibit dsDNA binding, reveals mechanistic details underlying target recognition and inhibition.
PubMed: 28985564
DOI: 10.1016/j.cell.2017.09.006
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.5 Å)
Structure validation

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