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Plos Biology : Draft Crystal Structure of the Vault Shell at 9-a° Resolution, Volume 5

By Petsko, Gregory A.

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Book Id: WPLBN0003926961
Format Type: PDF eBook :
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Reproduction Date: 2015

Title: Plos Biology : Draft Crystal Structure of the Vault Shell at 9-a° Resolution, Volume 5  
Author: Petsko, Gregory A.
Volume: Volume 5
Language: English
Subject: Journals, Science, Biology
Collections: Periodicals: Journal and Magazine Collection (Contemporary), PLoS Biology
Publication Date:
Publisher: Plos


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Petsko, G. A. (n.d.). Plos Biology : Draft Crystal Structure of the Vault Shell at 9-a° Resolution, Volume 5. Retrieved from

Description : Vaults are the largest known cytoplasmic ribonucleoprotein structures and may function in innate immunity. The vault shell self-assembles from 96 copies of major vault protein and encapsulates two other proteins and a small RNA. We crystallized rat liver vaults and several recombinant vaults, all among the largest non-icosahedral particles to have been crystallized. The best crystals thus far were formed from empty vaults built from a cysteine-tag construct of major vault protein (termed cpMVP vaults), diffracting to about 9-A° resolution. The asymmetric unit contains a half vault of molecular mass 4.65 MDa. X-ray phasing was initiated by molecular replacement, using density from cryo-electron microscopy (cryo-EM). Phases were improved by density modification, including concentric 24- and 48-fold rotational symmetry averaging. From this, the continuous cryo-EM electron density separated into domain-like blocks. A draft atomic model of cpMVP was fit to this improved density from 15 domain models. Three domains were adapted from a nuclear magnetic resonance substructure. Nine domain models originated in ab initio tertiary structure prediction. Three C-terminal domains were built by fitting poly-alanine to the electron density. Locations of loops in this model provide sites to test vault functions and to exploit vaults as nanocapsules.


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