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Cryo-EM structure and in vitro DNA packaging of a thermophilic virus with supersized T=7 capsids

DOI: 10.1073/pnas.1813204116 DOI Help

Authors: Oliver W. Bayfield (University of York; National Institute of Arthritis Musculoskeletal and Skin Diseases, National Institutes of Health) , Evgeny Klimuk (Skolkovo Institute of Science and Technology; Institute of Molecular Genetics, Russian Academy of Sciences) , Dennis C. Winkler (National Institute of Arthritis Musculoskeletal and Skin Diseases, National Institutes of Health) , Emma L. Hesketh (University of Leeds) , Maria Chechik (University of York) , Naiqian Cheng (National Institute of Arthritis Musculoskeletal and Skin Diseases, National Institutes of Health) , Eric C. Dykeman (University of York) , Leonid Minakhin (Waksman Institute for Microbiology, Rutgers, The State University of New Jersey) , Neil A. Ranson (University of Leeds) , Konstantin Severinov (Skolkovo Institute of Science and Technology; Institute of Molecular Genetics, Russian Academy of Sciences; Waksman Institute for Microbiology, Rutgers, The State University of New Jersey) , Alasdair C. Steven (University of York) , Alfred A. Antson (University of York)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Proceedings Of The National Academy Of Sciences , VOL 116 , PAGES 3556 - 3561

State: Published (Approved)
Published: February 2019
Diamond Proposal Number(s): 13587

Open Access Open Access

Abstract: Understanding molecular events during virus assembly and genome packaging is important for understanding viral life cycles, and the functioning of other protein–nucleic acid machines. The model system developed for the thermophilic bacteriophage P23-45 offers advantages over other systems. Cryo-EM reconstructions reveal modifications to a canonical capsid protein fold, resulting in capsids that are abnormally large for this virus class. Structural information on the portal protein, through which the genome is packaged, demonstrates that the capsid influences the portal’s conformation. This has implications for understanding how processes inside and outside the capsid can be coordinated.

Journal Keywords: virus assembly; DNA packaging; capsid; portal protein; cryo-EM

Subject Areas: Biology and Bio-materials


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)

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3556.full.pdf

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