Structure of a 16-nm Cage Designed by Using Protein Oligomers

Lai, Yen‐Ting; Cascio, Duilio; Yeates, Todd O.

doi:10.1126/science.1219351

Cited by 269 publications

(273 citation statements)

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“…Control SuPrA protomers containing entirely Ceru+32, entirely GFP-17, or an octamer of Ceru+32 juxtaposed with an octamer of GFP-17 were unstable at all NaCl concentrations, consistent with the experimental observations ( Supplementary Fig. 12, 13) Finer-grained structural modeling (i.e., of hydrophobic effects and counterion release) must await specific structural and physical details that should become manifest with further imaging (i.e., cryo-EM) experiments that better determine the precise symmetric arrangement of monomers.While previous studies have shown that it is possible to design synthetic protein oligomers either by modifying extant structures [13][14][15][16] or de novo, [8][9][10][11][12] we now show that it may be possible to induce the formation of novel quaternary structures through the simple expedient of supercharging. In so doing, we demonstrate that precise molecular configurations can be obtained by focusing on the driving forces for assembly (charge:charge interactions) rather than the details of the interface.…”

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Supercharging enables organized assembly of synthetic biomolecules

Simon

Ramasubramani

Gläser

et al. 2018

Preprint

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Abstract:There are few methods for the assembly of defined protein oligomers and higher order structures that could serve as novel biomaterials. Using fluorescent proteins as a model system, we have engineered novel oligomerization states by combining oppositely supercharged variants. A well-defined, highly symmetrical 16-mer (two stacked, circular octamers) can be formed from alternating charged proteins; higher order structures then form in a hierarchical fashion from this discrete protomer. During SUpercharged PRotein Assembly (SuPrA), electrostatic attraction between oppositely charged variants drives interaction, while shape and patchy physicochemical interactions lead to spatial organization along specific interfaces, ultimately resulting in protein assemblies never before seen in nature.All rights reserved. No reuse allowed without permission.(which was not peer-reviewed) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity.The copyright holder for this preprint . http://dx.doi.org/10.1101/323261 doi: bioRxiv preprint first posted online May. 16, 2018; 2 The assembly of genetically-encoded molecules into symmetric, supramolecular materials enables complex functions in natural biosystems and would likewise prove valuable in the development of bionanotechnologies including drug delivery, energy transport, and biological information storage. [1][2][3][4][5][6][7] Repeated, symmetric interactions between molecular building blocks enable the formation of complex, defined, assemblies from a small total number of components as well as dynamic propagation of conformational change. [3][4][5][6][7][8] However, while de novo engineering of artificial symmetrical biomolecular complexes has begun to be explored, 9-15 these efforts generally rely upon precise design of molecular interfaces. 16,17 In contrast, studies of simple synthetic colloids suggests that higher order structures can be derived based solely on packing and energetic and considerations. Computational and experimental studies of polyhedral or spherical colloids indicate that complementary particle shapes 18-24 and simple attractive "patches" [24][25][26][27][28][29] alone can enable formation of complex symmetrical assemblies. Shape complementarity has likewise been exploited to arrange synthetic linear biomolecules, i.e., double-stranded DNA strands, into distinct structures, demonstrating its utility for for the higher order arrangement of synthetic linear biomolecules, suggesting a utility beyond inorganic systems. 30,31Herein we demonstrate a simple, robust strategy to assemble normally monomeric proteins into well defined, oligomeric quaternary structures and micron-scale particles. This strategy centers on driving protein interactions by engineering oppositely supercharged variants. Generally, oppositely-charged proteins interact through simple electrostativ interactions. 32 Previously, this propensity has been exploited in artificial biosystems to engineer binary protein crystals from naturally oppos...

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mentioning

confidence: 99%

Supercharging enables organized assembly of synthetic biomolecules

Simon

Ramasubramani

Gläser

et al. 2018

Preprint

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“…Algumas descrições eram mais precisas e relatavam estudos sobre nanotubos de carbono (Baughman, 2000;Service, 2000;Dresselhaus, 2001;Gogotsi, Simon, 2011), nanotubos de DNA (Yin et al, 2008), nanopartículas metálicas (Buriak, 2004;Service, 2005a;Schliehe et al, 2010), nanocápsulas cristalinas (Buriak, 2004), por exemplo; outras abordavam um panorama mais amplo sobre a possibilidade de produzir novos materiais a partir da manipulação nos níveis atômico e molecular (Besenbacher, Norskov, 2000;Service, 2002;Parak, 2011, Lai et al, 2012.…”

Section: Figura 6 áReas De Aplicação Nanotecnológicaunclassified

“…Os mesmos relatos descrevem a felicidade dos pesquisadores (Proffitt, 2004), sua empolgação (Cho, 2006;Aldaye et al, 2008, Shalaev, 2008Brongersma, Shalaev, 2010;Boltasseva, Atwater, 2011;Hamburg, 2012) e seu fascínio (Dzenis, 2004;Shalaev, 2008;Parak, 2011) pela performance (Osborne, Clery, 2004;Ruiz et al, 2008;Brongersma, Shalaev, 2010), pela beleza (Murphy, 2002;Cho, 2006;Schliehe et al, 2010;Service, 2011) e perfeição (Forró, 2000;Siegel, 2004;Ruiz et al, 2008;Lai et al, 2012) de seus resultados. A descrição da nanotecnologia desta forma entusiasta não é sem propósito e reforça a capacidade que o discurso científico tem de revelar ou ocultar algum aspecto de sua atividade para o público em geral (Latour, 2000).…”

Section: A Escolha Dos Termos No Discurso Científicounclassified

“…No entanto, a fala que descreve os especializados métodos de organização e construção de estruturas descritas como complexas, harmoniosas, ornadas e perfeitas (Forró, 2000;Niemeyer, 2002;Buriak, 2004;Arslan et al, 2005;Ruiz et al, 2008;Liu, Yan, 2009;Lai et al, 2012;Service, 2005a) contrasta com aquela de que os métodos ainda não estão perfeitamente constituídos, e que a nanotecnologia traz riscos e precisa ter seus objetivos e instrumentos melhor estabelecidos e padronizados (Sigel et al, 2002;Bai, 2005;Service, 2005e;Holden, 2007).…”

Section: Perfeição X Riscounclassified

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Nanotecnociência e Humanidade

Pyrrho¹,

Schrram²

2016

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A navegação consulta e descarregamento dos títulos inseridos nas Bibliotecas Digitais UC Digitalis, UC Pombalina e UC Impactum, pressupõem a aceitação plena e sem reservas dos Termos e Condições de Uso destas Bibliotecas Digitais, disponíveis em https://digitalis.uc.pt/pt-pt/termos.Conforme exposto nos referidos Termos e Condições de Uso, o descarregamento de títulos de acesso restrito requer uma licença válida de autorização devendo o utilizador aceder ao(s) documento(s) a partir de um endereço de IP da instituição detentora da supramencionada licença.Ao utilizador é apenas permitido o descarregamento para uso pessoal, pelo que o emprego do(s) título(s) descarregado(s) para outro fim, designadamente comercial, carece de autorização do respetivo autor ou editor da obra. Na medida em que todas as obras da UC Digitalis se encontram protegidas pelo Código do Direito de Autor e Direitos Conexos e demais legislação aplicável, toda a cópia, parcial ou total, deste documento, nos casos em que é legalmente admitida, deverá conter ou fazer-se acompanhar por este aviso.

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“…We now have experimental data on the assembly, structure, dynamics and function of a wide range of protein complexes, ranging from small complexes such as haemoglobin 4,5 to large macromolecular machines such as the proteasome [6][7][8] . Furthermore, structurebased protein complex design has become feasible in certain cases [9][10][11][12] . Finally, structural bioinformatic approaches combined with mass spectrometry have revealed that most complexes assemble via ordered pathways that are generally conserved, and that show striking similarities to their evolutionary pathways [13][14][15] .…”

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Structural and evolutionary versatility in protein complexes with uneven stoichiometry

et al. 2015

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Proteins assemble into complexes with diverse quaternary structures. Although most heteromeric complexes of known structure have even stoichiometry, a significant minority have uneven stoichiometry-that is, differing numbers of each subunit type. To adopt this uneven stoichiometry, sequence-identical subunits must be asymmetric with respect to each other, forming different interactions within the complex. Here we first investigate the occurrence of uneven stoichiometry, demonstrating that it is common in vitro and is likely to be common in vivo. Next, we elucidate the structural determinants of uneven stoichiometry, identifying six different mechanisms by which it can be achieved. Finally, we study the frequency of uneven stoichiometry across evolution, observing a significant enrichment in bacteria compared with eukaryotes. We show that this arises due to a general increased tendency for bacterial proteins to self-assemble and form homomeric interactions, even within the context of a heteromeric complex.

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Structure of a 16-nm Cage Designed by Using Protein Oligomers

Cited by 269 publications

References 16 publications

Supercharging enables organized assembly of synthetic biomolecules

Supercharging enables organized assembly of synthetic biomolecules

Nanotecnociência e Humanidade

Structural and evolutionary versatility in protein complexes with uneven stoichiometry

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