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Structural plasticity enables evolution and innovation of rubisco assemblies

Research output: Contribution to Journal/Magazine › Journal article › peer-review

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Structural plasticity enables evolution and innovation of rubisco assemblies. / Liu, Albert K; Pereira, Jose H; Kehl, Alexander J. et al.
In: Science Advances, Vol. 8, No. 34, eadc9440, 26.08.2022.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Liu, AK, Pereira, JH, Kehl, AJ, Rosenberg, D, Orr, D, Chu, SKS, Banda, DM, Hammel, M, Adams, PD, Siegel, JB & Shih, PM 2022, 'Structural plasticity enables evolution and innovation of rubisco assemblies', Science Advances, vol. 8, no. 34, eadc9440. https://doi.org/10.1126/sciadv.adc9440

APA

Liu, A. K., Pereira, J. H., Kehl, A. J., Rosenberg, D., Orr, D., Chu, S. K. S., Banda, D. M., Hammel, M., Adams, P. D., Siegel, J. B., & Shih, P. M. (2022). Structural plasticity enables evolution and innovation of rubisco assemblies. Science Advances, 8(34), Article eadc9440. https://doi.org/10.1126/sciadv.adc9440

Vancouver

Liu AK, Pereira JH, Kehl AJ, Rosenberg D, Orr D, Chu SKS et al. Structural plasticity enables evolution and innovation of rubisco assemblies. Science Advances. 2022 Aug 26;8(34):eadc9440. doi: 10.1126/sciadv.adc9440

Author

Liu, Albert K ; Pereira, Jose H ; Kehl, Alexander J. et al. / Structural plasticity enables evolution and innovation of rubisco assemblies. In: Science Advances. 2022 ; Vol. 8, No. 34.

Bibtex

@article{0222e539f5474fc9af6c09badd93bcf9,
title = "Structural plasticity enables evolution and innovation of rubisco assemblies",
abstract = "Oligomerization is a core structural feature that defines the form and function of many proteins. Most proteins form molecular complexes; however, there remains a dearth of diversity-driven structural studies investigating the evolutionary trajectory of these assemblies. Ribulose-1,5-bisphosphate carboxylase-oxygenase (RuBisCO) is one such enzyme that adopts multiple assemblies, although the origins and distribution of its different oligomeric states remain cryptic. Here, we retrace the evolution of ancestral and extant form II RuBisCOs, revealing a complex and diverse history of oligomerization. We structurally characterize a newly discovered tetrameric RuBisCO, elucidating how solvent-exposed surfaces can readily adopt new interactions to interconvert or give rise to new oligomeric states. We further use these principles to engineer and demonstrate how changes in oligomerization can be mediated by relatively few mutations. Our findings yield insight into how structural plasticity may give rise to new oligomeric states.",
author = "Liu, {Albert K} and Pereira, {Jose H} and Kehl, {Alexander J.} and Daniel Rosenberg and Douglas Orr and Chu, {Simon K.S.} and Banda, {Douglas M} and Michal Hammel and Adams, {Paul D} and Siegel, {Justin B.} and Shih, {Patrick M}",
year = "2022",
month = aug,
day = "26",
doi = "10.1126/sciadv.adc9440",
language = "English",
volume = "8",
journal = "Science Advances",
issn = "2375-2548",
publisher = "American Association for the Advancement of Science",
number = "34",

}

RIS

TY - JOUR

T1 - Structural plasticity enables evolution and innovation of rubisco assemblies

AU - Liu, Albert K

AU - Pereira, Jose H

AU - Kehl, Alexander J.

AU - Rosenberg, Daniel

AU - Orr, Douglas

AU - Chu, Simon K.S.

AU - Banda, Douglas M

AU - Hammel, Michal

AU - Adams, Paul D

AU - Siegel, Justin B.

AU - Shih, Patrick M

PY - 2022/8/26

Y1 - 2022/8/26

N2 - Oligomerization is a core structural feature that defines the form and function of many proteins. Most proteins form molecular complexes; however, there remains a dearth of diversity-driven structural studies investigating the evolutionary trajectory of these assemblies. Ribulose-1,5-bisphosphate carboxylase-oxygenase (RuBisCO) is one such enzyme that adopts multiple assemblies, although the origins and distribution of its different oligomeric states remain cryptic. Here, we retrace the evolution of ancestral and extant form II RuBisCOs, revealing a complex and diverse history of oligomerization. We structurally characterize a newly discovered tetrameric RuBisCO, elucidating how solvent-exposed surfaces can readily adopt new interactions to interconvert or give rise to new oligomeric states. We further use these principles to engineer and demonstrate how changes in oligomerization can be mediated by relatively few mutations. Our findings yield insight into how structural plasticity may give rise to new oligomeric states.

AB - Oligomerization is a core structural feature that defines the form and function of many proteins. Most proteins form molecular complexes; however, there remains a dearth of diversity-driven structural studies investigating the evolutionary trajectory of these assemblies. Ribulose-1,5-bisphosphate carboxylase-oxygenase (RuBisCO) is one such enzyme that adopts multiple assemblies, although the origins and distribution of its different oligomeric states remain cryptic. Here, we retrace the evolution of ancestral and extant form II RuBisCOs, revealing a complex and diverse history of oligomerization. We structurally characterize a newly discovered tetrameric RuBisCO, elucidating how solvent-exposed surfaces can readily adopt new interactions to interconvert or give rise to new oligomeric states. We further use these principles to engineer and demonstrate how changes in oligomerization can be mediated by relatively few mutations. Our findings yield insight into how structural plasticity may give rise to new oligomeric states.

U2 - 10.1126/sciadv.adc9440

DO - 10.1126/sciadv.adc9440

M3 - Journal article

VL - 8

JO - Science Advances

JF - Science Advances

SN - 2375-2548

IS - 34

M1 - eadc9440

ER -