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The Trimeric Major Capsid Protein of Mavirus is stabilized by its Interlocked N-termini Enabling Core Flexibility for Capsid Assembly

Christiansen, Alexander; Weiel, Marie; Winkler, Andreas; Schug, Alexander; Reinstein, Jochen

Icosahedral viral capsids assemble with high fidelity from a large number of identical buildings blocks. The mechanisms that enable individual capsid proteins to form stable oligomeric units (capsomers) while affording structural adaptability required for further assembly into capsids are mostly unknown.

Understanding these mechanisms requires knowledge of the capsomers’ dynamics, especially for viruses where no additional helper proteins are needed during capsid assembly like for the Mavirus virophage that despite its complexity (triangulation number T = 27) can assemble from its major capsid protein (MCP) alone. This protein forms the basic building block of the capsid namely a trimer (MCP$_{3}$) of double-jelly roll protomers with highly intertwined N-terminal arms of each protomer wrapping around the other two at the base of the capsomer, secured by a clasp that is formed by part of the C-terminus.

Probing the dynamics of the capsomer with HDX mass spectrometry we observed differences in conformational flexibility between functional elements of the MCP trimer. While the N-terminal arm and clasp regions show above average deuterium incorporation, the two jelly-roll units in each protomer also differ in their structural plasticity, which might be needed for efficient assembly. ... mehr

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Verlagsausgabe §
DOI: 10.5445/IR/1000130503
Veröffentlicht am 19.03.2021
DOI: 10.1016/j.jmb.2021.166859
Cover der Publikation
Zugehörige Institution(en) am KIT Steinbuch Centre for Computing (SCC)
Publikationstyp Zeitschriftenaufsatz
Publikationsjahr 2021
Sprache Englisch
Identifikator ISSN: 0022-2836, 1089-8638
KITopen-ID: 1000130503
Erschienen in Journal of Molecular Biology
Verlag Elsevier
Band 433
Heft 7
Seiten Art.-Nr.: 166859
Nachgewiesen in Scopus
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