9N5A

CryoEM structure of Azotobacter vinelandii bacterioferritin

9N5A の概要

• エントリーDOI: 10.2210/pdb9n5a/pdb
• EMDBエントリー: 48919
• 分子名称: Bacterioferritin, PROTOPORPHYRIN IX CONTAINING FE (2 entities in total)
• 機能のキーワード: metal storage, metal binding protein
• 由来する生物種: Azotobacter vinelandii
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 439363.62

構造登録者

Warmack, R.A. (登録日: 2025-02-03, 公開日: 2025-07-16, 最終更新日: 2025-07-30)

主引用文献

Shen, Y.,Maggiolo, A.O.,Zhang, T.,Warmack, R.A.
CryoEM-enabled visual proteomics reveals de novo structures of oligomeric protein complexes.
Structure, 2025

PubMed Abstract: Single particle cryoelectron microscopy (cryoEM) and cryoelectron tomography (cryoET) are powerful methods for unveiling unique and functionally relevant structural states. Aided by mass spectrometry and machine learning, they promise to facilitate the visual exploration of proteomes. Leveraging visual proteomics, we interrogate structures isolated from a complex cellular milieu by cryoEM to identify and classify molecular structures and complexes de novo. By comparing three automated model building programs, CryoID, DeepTracer, and ModelAngelo, we determine the identity of six distinct oligomeric protein complexes from partially purified extracts of the nitrogen-fixing bacterium Azotobacter vinelandii using both anaerobic and aerobic cryoEM, including two original oligomeric structures. Overall, by allowing the study of near-native oligomeric protein states, cryoEM-enabled visual proteomics reveals unique structures that correspond to relevant species observed in situ.

PubMed: 40664216
DOI: 10.1016/j.str.2025.06.007

実験手法

ELECTRON MICROSCOPY (2.96 Å)