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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/46173

Title: Atomic structure of the 75 MDa extremophile Sulfolobus turreted icosahedral virus determined by CryoEM and X-ray crystallography.
Authors: avid Veesler
Thiam-Seng Ng
Anoop K. Sendamarai
Brian J. Eilers
C. Martin Lawrence
Shee-Mei Lok
Mark J. Young
John E. Johnson
Chi-yu Fu
Contributors: 國立臺灣海洋大學:海洋生物研究所
Keywords: PRD1-Adeno viral lineage
electron microscopy
Archaea
virus assembly
single-particle reconstruction
Date: 2013
Issue Date: 2018-05-07T06:06:33Z
Publisher: PNAS January
Abstract: Abstract
Sulfolobus turreted icosahedral virus (STIV) was isolated in acidic hot springs where it infects the archeon Sulfolobus solfataricus. We determined the STIV structure using near-atomic resolution electron microscopy and X-ray crystallography allowing tracing of structural polypeptide chains and visualization of transmembrane proteins embedded in the viral membrane. We propose that the vertex complexes orchestrate virion assembly by coordinating interactions of the membrane and various protein components involved. STIV shares the same coat subunit and penton base protein folds as some eukaryotic and bacterial viruses, suggesting that they derive from a common ancestor predating the divergence of the three kingdoms of life. One architectural motif (β-jelly roll fold) forms virtually the entire capsid (distributed in three different gene products), indicating that a single ancestral protein module may have been at the origin of its evolution.
Relation: 110(14)
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/46173
Appears in Collections:[海洋生物研究所] 期刊論文

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