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Literature summary for 1.8.7.2 extracted from

  • Dai, S.; Friemann, R.; Glauser, D.A.; Bourquin, F.; Manieri, W.; Schurmann, P.; Eklund, H.
    Structural snapshots along the reaction pathway of ferredoxin-thioredoxin reductase (2007), Nature, 448, 92-96.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
structures of FTR in both its one- and its two-electron-reduced intermediate states and of four complexes in the pathway. In the first complex of the pathway, ferredoxin-FTR, the ferredoxin [2Fe-2S] cluster is positioned suitably for electron transfer to the FTR [4Fe-4S] center. After the transfer of one electron, an intermediate is formed in which one sulfur atom of the FTR active site is free to attack a disulphide bridge in thioredoxin and the other sulfur atom forms a fifth ligand for an iron atom in the FTR [4Fe-4S] center. Ferredoxin then delivers a second electron that cleaves the FTR-thioredoxin heterodisulfide bond, which occurs in the ferredoxin-FTR-thioredoxin complex. In this structure, the redox centers of the three proteins are aligned to maximize the efficiency of electron transfer from the Fdx [2Fe-2S] cluster to the active-site disulfide of thioredoxin Synechocystis sp.

Organism

Organism UniProt Comment Textmining
Synechocystis sp.
-
PCC 6803
-