6OAW

Crystal structure of a CRISPR Cas-related protein

Summary for 6OAW

• Entry DOI: 10.2210/pdb6oaw/pdb
• Descriptor: WYL1, UNKNOWN ATOM OR ION (3 entities in total)
• Functional Keywords: wyl domain, structural genomics, structural genomics consortium, sgc, immune system
• Biological source: Ruminococcus sp.
• Total number of polymer chains: 2
• Total formula weight: 91988.43

Authors

Zhang, H.,Dong, C.,Li, L.,Tempel, W.,Bountra, C.,Arrowsmith, C.H.,Edwards, A.M.,Min, J.,Structural Genomics Consortium,Structural Genomics Consortium (SGC) (deposition date: 2019-03-18, release date: 2019-04-10, Last modification date: 2024-10-23)

Primary citation

Zhang, H.,Dong, C.,Li, L.,Wasney, G.A.,Min, J.
Structural insights into the modulatory role of the accessory protein WYL1 in the Type VI-D CRISPR-Cas system.
Nucleic Acids Res., 47:5420-5428, 2019

PubMed Abstract: The Type VI-D CRISPR-Cas system employs an RNA-guided RNase Cas13d with minimal targeting constraints to combat viral infections. This CRISPR system contains RspWYL1 as a unique accessory protein that plays a key role in boosting its effector function on target RNAs, but the mechanism behind this RspWYL1-mediated stimulation remains completely unexplored. Through structural and biophysical approaches, we reveal that the full-length RspWYL1 possesses a novel three-domain architecture and preferentially binds ssRNA with high affinity. Specifically, the N-terminus of RspWYL1 harbors a ribbon-helix-helix motif reminiscent of transcriptional regulators; the central WYL domain of RspWYL1 displays a Sm-like β-barrel fold; and the C-terminal domain of RspWYL1 primarily contributes to the dimerization of RspWYL1 and may regulate the RspWYL1 function via a large conformational change. Collectively, this study provides a first glimpse into the complex mechanism behind the RspWYL1-dictated boosting of target ssRNA cleavage in the Type VI-D CRISPR-Cas system.

PubMed: 30976796
DOI: 10.1093/nar/gkz269

Experimental method

X-RAY DIFFRACTION (2.2 Å)