Please use this identifier to cite or link to this item: https://doi.org/10.1073/pnas.1300601110
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dc.titleAtomic structure of the 75 MDa extremophile Sulfolobus turreted icosahedral virus determined by CryoEM and X-ray crystallography
dc.contributor.authorVeesler, D.
dc.contributor.authorNg, T.-S.
dc.contributor.authorSendamarai, A.K.
dc.contributor.authorEilers, B.J.
dc.contributor.authorLawrence, C.M.
dc.contributor.authorLok, S.-M.
dc.contributor.authorYoung, M.J.
dc.contributor.authorJohnson, J.E.
dc.contributor.authorFu, C.-Y.
dc.date.accessioned2016-09-06T02:59:38Z
dc.date.available2016-09-06T02:59:38Z
dc.date.issued2013-04-02
dc.identifier.citationVeesler, 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
dc.identifier.issn00278424
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/126468
dc.description.abstractSulfolobus 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.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1073/pnas.1300601110
dc.sourceScopus
dc.subjectArchaea
dc.subjectElectron microscopy
dc.subjectPRD1-Adeno viral lineage
dc.subjectSingle-particle reconstruction
dc.subjectVirus assembly
dc.typeArticle
dc.contributor.departmentDUKE-NUS GRADUATE MEDICAL SCHOOL S'PORE
dc.description.doi10.1073/pnas.1300601110
dc.description.sourcetitleProceedings of the National Academy of Sciences of the United States of America
dc.description.volume110
dc.description.issue14
dc.description.page5504-5509
dc.description.codenPNASA
dc.identifier.isiut000318037800061
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