caa a22 4500 528785990 20190713030955.0 cr unu---uuuuu 180924s2017 xx s 000 0 eng 10.3929/ethz-b-000129651 doi 10.1038/ncomms14663 doi (ETHRESEARCH)oai:www.research-collection.ethz.ch:20.500.11850/129651 Structure and assembly of scalable porous protein cages [Elektronische Daten] [Eita Sasaki, Daniel Böhringer, Michiel Van de Waterbeemd, Marc Leibundgut, Reinhard Zschoche, Albert J.R. Heck, Nenad Ban, Donald Hilvert] Nat Commun Open access ethresearch Proteins that self-assemble into regular shell-like polyhedra are useful, both in nature and in the laboratory, as molecular containers. Here we describe cryo-electron microscopy (EM) structures of two versatile encapsulation systems that exploit engineered electrostatic interactions for cargo loading. We show that increasing the number of negative charges on the lumenal surface of lumazine synthase, a protein that naturally assembles into a ∼1-MDa dodecahedron composed of 12 pentamers, induces stepwise expansion of the native protein shell, giving rise to thermostable ∼3-MDa and ∼6-MDa assemblies containing 180 and 360 subunits, respectively. Remarkably, these expanded particles assume unprecedented tetrahedrally and icosahedrally symmetric structures constructed entirely from pentameric units. Large keyhole-shaped pores in the shell, not present in the wild-type capsid, enable diffusion-limited encapsulation of complementarily charged guests. The structures of these supercharged assemblies demonstrate how programmed electrostatic effects can be effectively harnessed to tailor the architecture and properties of protein cages. Creative Commons Attribution 4.0 International http://creativecommons.org/licenses/by/4.0 ethresearch Sasaki Eita joint author Böhringer Daniel joint author Van de Waterbeemd Michiel joint author Leibundgut Marc joint author Zschoche Reinhard joint author Heck Albert J.R. joint author Ban Nenad joint author Hilvert Donald joint author Nature Communications London : Nature Publishing Group 8, p. 14663 2041-1723 http://hdl.handle.net/20.500.11850/129651 text/html WWW-Backlink auf das Repository (Open access) 1 Journal Article ethresearch ETHRESEARCH 856 40 http://hdl.handle.net/20.500.11850/129651 text/html WWW-Backlink auf das Repository (Open access) ETHRESEARCH 700 1- Sasaki Eita joint author ETHRESEARCH 700 1- Böhringer Daniel joint author ETHRESEARCH 700 1- Van de Waterbeemd Michiel joint author ETHRESEARCH 700 1- Leibundgut Marc joint author ETHRESEARCH 700 1- Zschoche Reinhard joint author ETHRESEARCH 700 1- Heck Albert J.R. joint author ETHRESEARCH 700 1- Ban Nenad joint author ETHRESEARCH 700 1- Hilvert Donald joint author ETHRESEARCH 773 0- Nature Communications London : Nature Publishing Group 8, p. 14663 2041-1723 BK010053 XK010053 XK010000 ETHRESEARCH ETHRESEARCH ETHRESEARCH Journal Article Open access