Enhanced Sampling and Free Energy Methods to Study Protein Folding and Dynamics

Pravin, Muthuraja Arun

doi:10.1007/978-981-99-2079-2_9

Cited by 1 publication

(1 citation statement)

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“…Our analysis illustrates that RbcL cannot explore new conformations or folds when RbcS is present, locking RbcS in the RuBisCO complex. Further investigations utilizing enhanced sampling techniques would also help explore larger portions of the conformational space accessible to the RuBisCO complex [53,54].…”

Section: Rubiscomentioning

confidence: 99%

Ancestral structure prediction reveals the conformational impact of the RuBisCO small subunit across time

Amritkar,

Cuevas,

Kacar

2024

Preprint

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Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is an ancient protein critical for CO2-fixation and global biogeochemistry. Form-I RuBisCO complexes uniquely harbor small subunits that form a hexadecameric complex together with their large subunits. The small subunit protein is thought to have significantly contributed to RuBisCO s response to the atmospheric rise of O2 ~2.5 billion years ago, marking a pivotal point in the enzyme s evolutionary history. Here, we performed a comprehensive evolutionary analysis of extant and ancestral RuBisCO sequences and structures to explore the impact of the small subunit s earliest integration on the molecular dynamics of the overall complex. Our simulations suggest that the small subunit restricted the conformational variability of the large subunit early in its history, constraining the evolutionary trajectory of the Form-I RuBisCO. Molecular dynamics investigations of CO2 and O2 gas distribution around predicted ancient RuBisCOs suggest that a proposed CO2 reservoir role for the small subunit is not conserved throughout the enzyme s evolutionary history. The evolutionary and biophysical response of RuBisCO to changing atmospheric conditions on ancient Earth showcase multi-level and trackable responses of enzymes to environmental shifts over long timescales.

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Section: Rubiscomentioning

confidence: 99%