1D4C

CRYSTAL STRUCTURE OF THE UNCOMPLEXED FORM OF THE FLAVOCYTOCHROME C FUMARATE REDUCTASE OF SHEWANELLA PUTREFACIENS STRAIN MR-1

Summary for 1D4C

• Entry DOI: 10.2210/pdb1d4c/pdb
• Related: 1D4C 1D4D 1D4E
• Descriptor: FLAVOCYTOCHROME C FUMARATE REDUCTASE, HEME C, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
• Functional Keywords: tetraheme flavocytochrome c, oxidoreductase
• Biological source: Shewanella oneidensis
• Cellular location: Periplasm : P83223
• Total number of polymer chains: 4
• Total formula weight: 253225.37

Authors

Leys, D.,Tsapin, A.S.,Meyer, T.E.,Cusanovich, M.A.,Van Beeumen, J.J. (deposition date: 1999-10-03, release date: 1999-12-01, Last modification date: 2024-10-30)

Primary citation

Leys, D.,Tsapin, A.S.,Nealson, K.H.,Meyer, T.E.,Cusanovich, M.A.,Van Beeumen, J.J.
Structure and mechanism of the flavocytochrome c fumarate reductase of Shewanella putrefaciens MR-1.
Nat.Struct.Biol., 6:1113-1117, 1999

PubMed Abstract: Fumarate respiration is one of the most widespread types of anaerobic respiration. The soluble fumarate reductase of Shewanella putrefaciens MR-1 is a periplasmic tetraheme flavocytochrome c. The crystal structures of the enzyme were solved to 2.9 A for the uncomplexed form and to 2.8 A and 2.5 A for the fumarate and the succinate-bound protein, respectively. The structures reveal a flexible capping domain linked to the FAD-binding domain. A catalytic mechanism for fumarate reduction based on the structure of the complexed protein is proposed. The mechanism for the reverse reaction is a model for the homologous succinate dehydrogenase (complex II) of the respiratory chain. In flavocytochrome c fumarate reductase, all redox centers are in van der Waals contact with one another, thus providing an efficient conduit of electrons from the hemes via the FAD to fumarate.

PubMed: 10581551
DOI: 10.1038/70051

Experimental method

X-RAY DIFFRACTION (2.9 Å)