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3J31

Life in the extremes: atomic structure of Sulfolobus Turreted Icosahedral Virus

Summary for 3J31
Entry DOI10.2210/pdb3j31/pdb
EMDB information5584
DescriptorA223 penton base, A55 membrane protein, Coat protein, ... (4 entities in total)
Functional Keywordsvirus assembly, evolution, archaea, virus
Biological sourceSulfolobus turreted icosahedral virus (STIV)
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Total number of polymer chains18
Total formula weight635323.06
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. (deposition date: 2013-02-18, release date: 2013-05-01, Last modification date: 2024-02-21)
Primary 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.
Atomic structure of the 75 MDa extremophile Sulfolobus turreted icosahedral virus determined by CryoEM and X-ray crystallography.
Proc.Natl.Acad.Sci.USA, 110:5504-5509, 2013
Cited by
PubMed 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.
PubMed: 23520050
DOI: 10.1073/pnas.1300601110
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.5 Å)
Structure validation

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