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Atomic structure of the 75 MDa extremophile Sulfolobus turreted icosahedral virus determined by CryoEM and X-ray crystallography

Academic Article
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Overview

authors

  • Veesler, D.
  • Ng, T. S.
  • Sendamarai, A. K.
  • Eilers, B. J.
  • Lawrence, C. M.
  • Lok, S. M.
  • Young, M. J.
  • Johnson Jr., John
  • Fu, C. Y.

publication date

  • April 2013

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

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 (?-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.
  • 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.

subject areas

  • Cryoelectron Microscopy
  • Crystallography, X-Ray
  • Membrane Proteins
  • Models, Molecular
  • Rudiviridae
  • Sulfolobus
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Research

keywords

  • Archaea
  • PRD1-Adeno viral lineage
  • electron microscopy
  • single-particle reconstruction
  • virus assembly
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Identity

PubMed Central ID

  • PMC3619359

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.1300601110

PubMed ID

  • 23520050
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Additional Document Info

start page

  • 5504

end page

  • 5509

volume

  • 110

issue

  • 14

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