Structural changes in a marine podovirus associated with release of its genome into Prochlorococcus

被引:114
作者
Liu, Xiangan [1 ]
Zhang, Qinfen [1 ,2 ]
Murata, Kazuyoshi [1 ]
Baker, Matthew L. [1 ]
Sullivan, Matthew B. [3 ]
Fu, Caroline [1 ]
Dougherty, Matthew T. [1 ]
Schmid, Michael F. [1 ]
Osburne, Marcia S. [3 ]
Chisholm, Sallie W. [3 ]
Chiu, Wah [1 ]
机构
[1] Baylor Coll Med, Verna & Marrs Mclean Dept Biochem & Mol Biol, Natl Ctr Macromol Imaging, Houston, TX 77030 USA
[2] Sun Yat Sen Univ, Sch Life Sci, State Key Lab Biocontrol, Guangzhou 510275, Guangdong, Peoples R China
[3] MIT, Dept Civil & Environm Engn, Cambridge, MA 02139 USA
基金
美国国家科学基金会; 美国国家卫生研究院;
关键词
SECONDARY STRUCTURE ELEMENTS; STRUCTURE PREDICTION SERVER; ELECTRON CRYOMICROSCOPY; CRYOELECTRON MICROSCOPY; PROTEIN; BACTERIOPHAGES; RESOLUTION; MECHANISM; VIRUS; RECONSTRUCTION;
D O I
10.1038/nsmb.1823
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Podovirus P-SSP7 infects Prochlorococcus marinus, the most abundant oceanic photosynthetic microorganism. Single-particle cryo-electron microscopy yields icosahedral and asymmetrical structures of infectious P-SSP7 with 4.6-angstrom and 9-angstrom resolution, respectively. The asymmetric reconstruction reveals how symmetry mismatches are accommodated among five of the gene products at the portal vertex. Reconstructions of infectious and empty particles show a conformational change of the 'valve' density in the nozzle, an orientation difference in the tail fibers, a disordering of the C terminus of the portal protein and the disappearance of the core proteins. In addition, cryo-electron tomography of P-SSP7 infecting Prochlorococcus showed the same tail-fiber conformation as that in empty particles. Our observations suggest a mechanism whereby, upon binding to the host cell, the tail fibers induce a cascade of structural alterations of the portal vertex complex that triggers DNA release.
引用
收藏
页码:830 / U76
页数:8
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