8QMW

Non-obligately L8S8-complex forming RubisCO derived from ancestral sequence reconstruction and rational engineering in L8S8 complex with substitutions R269W, E271R, L273N

8QMW の概要

• エントリーDOI: 10.2210/pdb8qmw/pdb
• 分子名称: RubisCO large subunit, RubisCO small subunit, 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: rubisco, cabp, ancestral, lyase
• 由来する生物種: synthetic construct; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 256346.85

構造登録者

Zarzycki, J.,Schulz, L.,Erb, T.J.,Hochberg, G.K.A. (登録日: 2023-09-25, 公開日: 2024-10-02, 最終更新日: 2025-01-15)

主引用文献

Schulz, L.,Zarzycki, J.,Steinchen, W.,Hochberg, G.K.A.,Erb, T.J.
Layered entrenchment maintains essentiality in the evolution of Form I Rubisco complexes.
Embo J., 44:269-280, 2025

PubMed Abstract: Protein complexes composed of strictly essential subunits are abundant in nature and often arise through the gradual complexification of ancestral precursor proteins. Essentiality can arise through the accumulation of changes that are tolerated in the complex state but would be deleterious for the standalone complex components. While this theoretical framework to explain how essentiality arises has been proposed long ago, it is unclear which factors cause essentiality to persist over evolutionary timescales. In this work we show that the central enzyme of photosynthesis, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), can easily start to depend on a newly recruited interaction partner through multiple, genetically distinct mechanisms that affect stability, solubility, and catalysis. We demonstrate that layering multiple mechanisms of essentiality can lead to its persistence, even if any given mechanism reverts. More broadly, our work highlights that new interaction partners can drastically re-shape which substitutions are tolerated in the proteins they are recruited into. This can lead to the evolution of multilayered essentiality through the exploration of areas of sequence space that are only accessible in the complex state.

PubMed: 39558108
DOI: 10.1038/s44318-024-00311-1

実験手法

X-RAY DIFFRACTION (1.75 Å)