Structural highlights
Publication Abstract from PubMed
Packaging of phage phi29 genome requires the ATPase gp16 and prohead RNA (pRNA). The highly conserved pRNA forms the interface between the connector complex and gp16. Understanding how pRNA interacts with gp16 under packaging conditions can shed light on the molecular mechanism of the packaging motor. Here, we present 3D models of the pRNA-gp16 complex and its conformation change in response to ATP or ADP binding. Using a combination of crystallography, small angle X-ray scattering and chemical probing, we find that the pRNA and gp16 forms a 'Z'-shaped complex, with gp16 specifically binds to pRNA domain II. The whole complex closes in the presence of ATP, and pRNA domain II rotates open as ATP hydrolyzes, before resetting after ADP is released. Our results suggest that pRNA domain II actively participates in the packaging process.
ATP/ADP modulates gp16-pRNA conformational change in the Phi29 DNA packaging motor.,Cai R, Price IR, Ding F, Wu F, Chen T, Zhang Y, Liu G, Jardine PJ, Lu C, Ke A Nucleic Acids Res. 2019 Aug 9. pii: 5545366. doi: 10.1093/nar/gkz692. PMID:31396619[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cai R, Price IR, Ding F, Wu F, Chen T, Zhang Y, Liu G, Jardine PJ, Lu C, Ke A. ATP/ADP modulates gp16-pRNA conformational change in the Phi29 DNA packaging motor. Nucleic Acids Res. 2019 Aug 9. pii: 5545366. doi: 10.1093/nar/gkz692. PMID:31396619 doi:http://dx.doi.org/10.1093/nar/gkz692
