5JBL

Structure of the bacteriophage T4 capsid assembly protease, gp21.

Summary for 5JBL

• Entry DOI: 10.2210/pdb5jbl/pdb
• Descriptor: Prohead core protein protease (2 entities in total)
• Functional Keywords: protease pentamer, phage t4, prohead, hydrolase
• Biological source: Enterobacteria phage T4
• Total number of polymer chains: 5
• Total formula weight: 126042.24

Authors

Fokine, A.,Rossmann, M.G. (deposition date: 2016-04-13, release date: 2016-12-07, Last modification date: 2024-03-06)

Primary citation

Fokine, A.,Rossmann, M.G.
Common Evolutionary Origin of Procapsid Proteases, Phage Tail Tubes, and Tubes of Bacterial Type VI Secretion Systems.
Structure, 24:1928-1935, 2016

PubMed Abstract: Many large viruses, including tailed dsDNA bacteriophages and herpesviruses, assemble their capsids via formation of precursors, called procapsids or proheads. The prohead has an internal core, made of scaffolding proteins, and an outer shell, formed by the major capsid protein. The prohead usually contains a protease, which is activated during capsid maturation to destroy the inner core and liberate space for the genome. Here, we report a 2.0 Å resolution structure of the pentameric procapsid protease of bacteriophage T4, gene product (gp)21. The structure corresponds to the enzyme's pre-active state in which its N-terminal region blocks the catalytic center, demonstrating that the activation mechanism involves self-cleavage of nine N-terminal residues. We describe similarities and differences between T4 gp21 and related herpesvirus proteases. We found that gp21 and the herpesvirus proteases have similarity with proteins forming the tubes of phage tails and bacterial type VI secretion systems, suggesting their common evolutionary origin.

PubMed: 27667692
DOI: 10.1016/j.str.2016.08.013

Experimental method

X-RAY DIFFRACTION (1.943 Å)