6ANV
Crystal structure of anti-CRISPR protein AcrF1
Summary for 6ANV
Entry DOI | 10.2210/pdb6anv/pdb |
Related PRD ID | PRD_900010 |
Descriptor | anti-CRISPR protein AcrF1 fused with C-terminal MBP tag, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (7 entities in total) |
Functional Keywords | type i-f crispr-cas system: csy cascade: structure: anti-crispr protein: inhibition of csy complex: genome editing tool, immune system |
Biological source | Pseudomonas phage JBD30 More |
Total number of polymer chains | 2 |
Total formula weight | 102897.75 |
Authors | Yang, H.,Patel, D.J. (deposition date: 2017-08-14, release date: 2017-10-25, Last modification date: 2023-10-04) |
Primary citation | Guo, 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: 28985564DOI: 10.1016/j.cell.2017.09.006 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.265 Å) |
Structure validation
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