ジャーナル: Mol Cell / 年: 2008 タイトル: A conformational switch in bacteriophage p22 portal protein primes genome injection. 著者: Hongjin Zheng / Adam S Olia / Melissa Gonen / Simeon Andrews / Gino Cingolani / Tamir Gonen / 要旨: Double-stranded DNA (dsDNA) viruses such as herpesviruses and bacteriophages infect by delivering their genetic material into cells, a task mediated by a DNA channel called "portal protein." We have ...Double-stranded DNA (dsDNA) viruses such as herpesviruses and bacteriophages infect by delivering their genetic material into cells, a task mediated by a DNA channel called "portal protein." We have used electron cryomicroscopy to determine the structure of bacteriophage P22 portal protein in both the procapsid and mature capsid conformations. We find that, just as the viral capsid undergoes major conformational changes during virus maturation, the portal protein switches conformation from a procapsid to a mature phage state upon binding of gp4, the factor that initiates tail assembly. This dramatic conformational change traverses the entire length of the DNA channel, from the outside of the virus to the inner shell, and erects a large dome domain directly above the DNA channel that binds dsDNA inside the capsid. We hypothesize that this conformational change primes dsDNA for injection and directly couples completion of virus morphogenesis to a new cycle of infection.
全体 : truncated portal complex with gp4 from bacteriophage P22
全体
名称: truncated portal complex with gp4 from bacteriophage P22
要素
試料: truncated portal complex with gp4 from bacteriophage P22
タンパク質・ペプチド: gp1, gp4
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超分子 #1000: truncated portal complex with gp4 from bacteriophage P22
超分子
名称: truncated portal complex with gp4 from bacteriophage P22 タイプ: sample / ID: 1000 / 集合状態: 12mer of portal with 12mer of gp4 / Number unique components: 2