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

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.

authors

Veesler D,Ng TS,Sendamarai AK,Eilers BJ,Lawrence CM,Lok SM,Young MJ,Johnson JE,Fu CY

doi

10.1073/pnas.1300601110

subject

Has Abstract

pub_date

2013-04-02 00:00:00

pages

5504-9

issue

14

eissn

0027-8424

issn

1091-6490

pii

1300601110

journal_volume

110

pub_type

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