7CNB

Crystal structure of Gp16 C-terminal domain from Bacillus virus phi29

Summary for 7CNB

• Entry DOI: 10.2210/pdb7cnb/pdb
• Descriptor: DNA packaging protein (1 entity in total)
• Functional Keywords: crystal structure of gp16 c-terminal domain from bacillus virus phi29, motor protein
• Biological source: Bacillus phage phi29
• Total number of polymer chains: 1
• Total formula weight: 12675.44

Authors

Ouyang, S.Y.,Saeed, A.F.U.H. (deposition date: 2020-07-30, release date: 2021-03-24, Last modification date: 2024-03-27)

Primary citation

Saeed, A.F.U.H.,Chan, C.,Guan, H.,Gong, B.,Guo, P.,Cheng, X.,Ouyang, S.
Structural Insights into gp16 ATPase in the Bacteriophage φ29 DNA Packaging Motor.
Biochemistry, 60:886-897, 2021

PubMed Abstract: Biological motors, ubiquitous in living systems, convert chemical energy into different kinds of mechanical motions critical to cellular functions. Gene product 16 (gp16) in bacteriophage ϕ29 is among the most powerful biomotors known, which adopts a multisubunit ring-shaped structure and hydrolyzes ATP to package double-stranded DNA (dsDNA) into a preformed procapsid. Here we report the crystal structure of the C-terminal domain of gp16 (gp16-CTD). Structure-based alignment and molecular dynamics simulations revealed an essential binding surface of gp16-CTD for prohead RNA, a unique component of the motor complex. Furthermore, our simulations highlighted a dynamic interplay between the N-terminal domain and the CTD of gp16, which may play a role in driving movement of DNA into the procapsid. Lastly, we assembled an atomic structural model of the complete ϕ29 dsDNA packaging motor complex by integrating structural and experimental data from multiple sources. Collectively, our findings provided a refined inchworm-revolution model for dsDNA translocation in bacteriophage ϕ29 and suggested how the individual domains of gp16 work together to power such translocation.

PubMed: 33689296
DOI: 10.1021/acs.biochem.0c00935

Experimental method

X-RAY DIFFRACTION (2.32 Å)