7PLM

CryoEM reconstruction of pyruvate ferredoxin oxidoreductase (PFOR) in anaerobic conditions

7PLM の概要

• エントリーDOI: 10.2210/pdb7plm/pdb
• 関連するPDBエントリー: 1B0P
• EMDBエントリー: 13493
• 分子名称: Pyruvate:ferredoxin oxidoreductase, IRON/SULFUR CLUSTER, THIAMINE DIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: 4fe-4s, anaerobic, pyruvate catabolism, electron transport, oxidoreductase
• 由来する生物種: Desulfocurvibacter africanus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 270759.45

構造登録者

Cherrier, M.V.,Vernede, X.,Fenel, D.,Martin, L.,Arragain, B.,Neumann, E.,Fontecilla Camps, J.C.,Schoehn, G.,Nicolet, Y. (登録日: 2021-08-31, 公開日: 2022-03-23, 最終更新日: 2024-11-13)

主引用文献

Cherrier, M.V.,Vernede, X.,Fenel, D.,Martin, L.,Arragain, B.,Neumann, E.,Fontecilla-Camps, J.C.,Schoehn, G.,Nicolet, Y.
Oxygen-Sensitive Metalloprotein Structure Determination by Cryo-Electron Microscopy.
Biomolecules, 12:-, 2022

PubMed Abstract: Metalloproteins are involved in key cell processes such as photosynthesis, respiration, and oxygen transport. However, the presence of transition metals (notably iron as a component of [Fe-S] clusters) often makes these proteins sensitive to oxygen-induced degradation. Consequently, their study usually requires strict anaerobic conditions. Although X-ray crystallography has been the method of choice for solving macromolecular structures for many years, recently electron microscopy has also become an increasingly powerful structure-solving technique. We have used our previous experience with cryo-crystallography to develop a method to prepare cryo-EM grids in an anaerobic chamber and have applied it to solve the structures of apoferritin and the 3 [FeS]-containing pyruvate ferredoxin oxidoreductase (PFOR) at 2.40 Å and 2.90 Å resolution, respectively. The maps are of similar quality to the ones obtained under air, thereby validating our method as an improvement in the structural investigation of oxygen-sensitive metalloproteins by cryo-EM.

PubMed: 35327633
DOI: 10.3390/biom12030441

実験手法

ELECTRON MICROSCOPY (2.9 Å)