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7PLM

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

Summary for 7PLM
Entry DOI10.2210/pdb7plm/pdb
Related1B0P
EMDB information13493
DescriptorPyruvate:ferredoxin oxidoreductase, IRON/SULFUR CLUSTER, THIAMINE DIPHOSPHATE, ... (6 entities in total)
Functional Keywords4fe-4s, anaerobic, pyruvate catabolism, electron transport, oxidoreductase
Biological sourceDesulfocurvibacter africanus
Total number of polymer chains2
Total formula weight270759.45
Authors
Cherrier, M.V.,Vernede, X.,Fenel, D.,Martin, L.,Arragain, B.,Neumann, E.,Fontecilla Camps, J.C.,Schoehn, G.,Nicolet, Y. (deposition date: 2021-08-31, release date: 2022-03-23, Last modification date: 2024-11-13)
Primary citationCherrier, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.9 Å)
Structure validation

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数据于2025-06-25公开中

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