9BT4
Pyruvate:Ferredoxin Oxidoreductase from Methanosarcina acetivorans
Summary for 9BT4
| Entry DOI | 10.2210/pdb9bt4/pdb |
| Descriptor | Pyruvate:Ferredoxin Oxidoreductase, subunit alpha, Pyruvate:Ferredoxin Oxidoreductase, subunit beta, Pyruvate:Ferredoxin Oxidoreductase, subunit delta, ... (8 entities in total) |
| Functional Keywords | oxidoreductase, electron transport |
| Biological source | Methanosarcina acetivorans C2A More |
| Total number of polymer chains | 8 |
| Total formula weight | 213728.14 |
| Authors | Catlin, D.,Nair, S.J. (deposition date: 2024-05-14, release date: 2024-10-09, Last modification date: 2024-11-27) |
| Primary citation | Cossu, M.,Catlin, D.,Elliott, S.J.,Metcalf, W.W.,Nair, S.K. Structural organization of pyruvate: ferredoxin oxidoreductase from the methanogenic archaeon Methanosarcina acetivorans. Structure, 32:1963-, 2024 Cited by PubMed Abstract: Enzymes of the 2-oxoacid:ferredoxin oxidoreductase (OFOR) superfamily catalyze the reversible oxidation of 2-oxoacids to acyl-coenzyme A esters and carbon dioxide (CO)using ferredoxin or flavodoxin as the redox partner. Although members of the family share primary sequence identity, a variety of domain and subunit arrangements are known. Here, we characterize the structure of a four-subunit family member: the pyruvate:ferredoxin oxidoreductase (PFOR) from the methane producing archaeon Methanosarcina acetivorans (MaPFOR). The 1.92 Å resolution crystal structure of MaPFOR shows a protein fold like those of single- or two-subunit PFORs that function in 2-oxoacid oxidation, including the location of the requisite thiamine pyrophosphate (TPP), and three [4Fe-4S] clusters. Of note, MaPFOR typically functions in the CO reductive direction, and structural comparisons to the pyruvate oxidizing PFORs show subtle differences in several regions of catalytical relevance. These studies provide a framework that may shed light on the biochemical mechanisms used to facilitate reductive pyruvate synthesis. PubMed: 39265575DOI: 10.1016/j.str.2024.08.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.92 Å) |
Structure validation
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