id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-356291-0x1jhya6	Tang, Liang	Three-dimensional structure of the bacteriophage P22 tail machine	2005-06-02		.txt	text/plain	6191	300	60	The three-dimensional structure of the P22 tail machine determined by electron cryo-microscopy and image reconstruction reveals how the five types of polypeptides present as 51 subunits are organized into this molecular machine through twelve-, sixand three-fold symmetry, and provides insights into molecular events during host cell attachment and phage DNA translocation. The electron cryo-microscopy (cryoEM) structure of Bacillus phage SPP1 portal in complex with head completion proteins gp15 and gp16, through which the tail is connected to the head, revealed local conformational change of the portal upon binding of gp15 and the function of gp16 as a valve (Orlova et al, 2003) . Here, we present the three-dimensional structures of the tail machine and a C-terminally truncated form of the portal protein of bacteriophage P22 determined by cryoEM and image reconstruction.	./cache/cord-356291-0x1jhya6.txt	./txt/cord-356291-0x1jhya6.txt