Please use this identifier to cite or link to this item: https://doi.org/10.1073/pnas.1300601110
Title: Atomic structure of the 75 MDa extremophile Sulfolobus turreted icosahedral virus determined by CryoEM and X-ray crystallography
Authors: Veesler, D.
Ng, T.-S. 
Sendamarai, A.K.
Eilers, B.J.
Lawrence, C.M.
Lok, S.-M. 
Young, M.J.
Johnson, J.E.
Fu, C.-Y.
Keywords: Archaea
Electron microscopy
PRD1-Adeno viral lineage
Single-particle reconstruction
Virus assembly
Issue Date: 2-Apr-2013
Citation: Veesler, D., Ng, T.-S., Sendamarai, A.K., Eilers, B.J., Lawrence, C.M., Lok, S.-M., Young, M.J., Johnson, J.E., Fu, C.-Y. (2013-04-02). Atomic structure of the 75 MDa extremophile Sulfolobus turreted icosahedral virus determined by CryoEM and X-ray crystallography. Proceedings of the National Academy of Sciences of the United States of America 110 (14) : 5504-5509. ScholarBank@NUS Repository. https://doi.org/10.1073/pnas.1300601110
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.
Source Title: Proceedings of the National Academy of Sciences of the United States of America
URI: http://scholarbank.nus.edu.sg/handle/10635/126468
ISSN: 00278424
DOI: 10.1073/pnas.1300601110
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