Structure and function of the small terminase component of the DNA packaging machine in T4-like bacteriophages.
Tailed DNA bacteriophages assemble empty procapsids that are subsequently filled with the viral genome by means of a DNA packaging machine situated at a special fivefold vertex. The packaging machine consists of a "small terminase" and a "large terminase" component. One of the functions of the small terminase is to initiate packaging of the viral genome, whereas the large terminase is responsible for the ATP-powered translocation of DNA. The small terminase subunit has three domains, an N-terminal DNA-binding domain, a central oligomerization domain, and a C-terminal domain for interacting with the large terminase. Here we report structures of the central domain in two different oligomerization states for a small terminase from the T4 family of phages. In addition, we report biochemical studies that establish the function for each of the small terminase domains. On the basis of the structural and biochemical information, we propose a model for DNA packaging initiation.
Department of Biological Sciences, Purdue University, 240 S. Martin Jischke Drive, West Lafayette, IN 47907-2032, USA.
Siyang
S
Sun
Song
S
Gao
Kiran
K
Kondabagil
Ye
Y
Xiang
Michael G
MG
Rossmann
Venigalla B
VB
Rao
D017122:Bacteriophage T4 / Q000201:enzymology*; D042003:DNA Packaging; D004706:Endodeoxyribonucleases / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship; D014764:Viral Proteins / Q000737:chemistry* / Q000378:metabolism*
D014764:Viral Proteins; D004706:Endodeoxyribonucleases; C030894:terminase