5WTJ

Crystal structure of an endonuclease

Summary for 5WTJ

• Entry DOI: 10.2210/pdb5wtj/pdb
• Related: 5WTK
• Descriptor: CRISPR-associated endoribonuclease C2c2 (2 entities in total)
• Functional Keywords: hydrolase
• Biological source: Leptotrichia shahii (strain DSM 19757 / CCUG 47503 / CIP 107916 / JCM 16776 / LB37)
• Total number of polymer chains: 2
• Total formula weight: 336749.91

Authors

Liu, L.,Wang, Y. (deposition date: 2016-12-13, release date: 2017-02-08, Last modification date: 2024-11-13)

Primary citation

Liu, L.,Li, X.,Wang, J.,Wang, M.,Chen, P.,Yin, M.,Li, J.,Sheng, G.,Wang, Y.
Two Distant Catalytic Sites Are Responsible for C2c2 RNase Activities
Cell, 168:121-134.e12, 2017

PubMed Abstract: C2c2, the effector of type VI CRISPR-Cas systems, has two RNase activities-one for cutting its RNA target and the other for processing the CRISPR RNA (crRNA). Here, we report the structures of Leptotrichia shahii C2c2 in its crRNA-free and crRNA-bound states. While C2c2 has a bilobed structure reminiscent of all other Class 2 effectors, it also exhibits different structural characteristics. It contains the REC lobe with a Helical-1 domain and the NUC lobe with two HEPN domains. The two RNase catalytic pockets responsible for cleaving pre-crRNA and target RNA are independently located on Helical-1 and HEPN domains, respectively. crRNA binding induces significant conformational changes that are likely to stabilize crRNA binding and facilitate target RNA recognition. These structures provide important insights into the molecular mechanism of dual RNase activities of C2c2 and establish a framework for its future engineering as a RNA editing tool.

PubMed: 28086085
DOI: 10.1016/j.cell.2016.12.031

Experimental method

X-RAY DIFFRACTION (3.503 Å)