9HBN

A. vinelandii nitrogenase MoFe protein Anc1b

9HBN の概要

• エントリーDOI: 10.2210/pdb9hbn/pdb
• 関連するPDBエントリー: 9HAZ 9HB9 9HBC
• 分子名称: MoFe nitrogenase subunit D, MoFe nitrogenase subunit K, iron-sulfur-molybdenum cluster with interstitial carbon, ... (9 entities in total)
• 機能のキーワード: nitrogen fixation, oxidoreductase
• 由来する生物種: Azotobacter vinelandii DJ; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 237018.52

構造登録者

Detemple, F.,Kacar, B.,Einsle, O. (登録日: 2024-11-07, 公開日: 2025-09-10, 最終更新日: 2025-10-01)

主引用文献

Cuevas Zuviria, B.,Detemple, F.,Amritkar, K.,Garcia, A.K.,Seefeldt, L.,Einsle, O.,Kacar, B.
Structural evolution of nitrogenase over 3 billion years.
Elife, 14:-, 2025

PubMed Abstract: Previously, we identified the only dinitrogen reduction mechanism known to date as an ancient feature conserved from nitrogenase ancestors, which we directly tested by resurrecting and integrating synthetic ancestral nitrogenases into the genome of (Garcia et al., 2023), a genetically tractable, nitrogen-fixing model bacterium. Here, we extend this paleomolecular approach to investigate the structural evolution of nitrogenase over billions of years of evolution by combining phylogenetics, ancestral sequence reconstruction, protein crystallography, and deep-learning based predictions. This study reveals that nitrogenase, while maintaining a conserved multimeric core, evolved novel modular features aligned with major environmental transitions, suggesting that subtle distal changes and transient regulatory adaptations were key to its long-term persistence and to shaping protein evolution over geologic time. The framework established here provides a foundation for identifying structural constraints that governed ancient proteins and for situating their sequences and structures within phylogenetic and environmental contexts across time.

PubMed: 40934104
DOI: 10.7554/eLife.105613

実験手法

X-RAY DIFFRACTION (1.824 Å)