1FCD

THE STRUCTURE OF FLAVOCYTOCHROME C SULFIDE DEHYDROGENASE FROM A PURPLE PHOTOTROPHIC BACTERIUM CHROMATIUM VINOSUM AT 2.5 ANGSTROMS RESOLUTION

Summary for 1FCD

• Entry DOI: 10.2210/pdb1fcd/pdb
• Descriptor: FLAVOCYTOCHROME C SULFIDE DEHYDROGENASE (FLAVIN-BINDING SUBUNIT), FLAVOCYTOCHROME C SULFIDE DEHYDROGENASE (CYTOCHROME SUBUNIT), FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: electron transport(flavocytochrome)
• Biological source: Allochromatium vinosum; More
• Cellular location: Periplasm: Q06530 Q06529
• Total number of polymer chains: 4
• Total formula weight: 128196.83

Authors

Chen, Z.W.,Koh, M.,Van Driessche, G.,Van Beeumen, J.J.,Bartsch, R.G.,Meyer, T.E.,Cusanovich, M.A.,Mathews, F.S. (deposition date: 1994-08-18, release date: 1994-11-01, Last modification date: 2024-10-09)

Primary citation

Chen, Z.W.,Koh, M.,Van Driessche, G.,Van Beeumen, J.J.,Bartsch, R.G.,Meyer, T.E.,Cusanovich, M.A.,Mathews, F.S.
The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium.
Science, 266:430-432, 1994

PubMed Abstract: The structure of the heterodimeric flavocytochrome c sulfide dehydrogenase from Chromatium vinosum was determined at a resolution of 2.53 angstroms. It contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit. The diheme cytochrome folds as two domains, each resembling mitochondrial cytochrome c, and has an unusual interpropionic acid linkage joining the two heme groups in the interior of the subunit. The active site of the flavoprotein subunit contains a catalytically important disulfide bridge located above the pyrimidine portion of the flavin ring. A tryptophan, threonine, or tyrosine side chain may provide a partial conduit for electron transfer to one of the heme groups located 10 angstroms from the flavin.

PubMed: 7939681

Experimental method

X-RAY DIFFRACTION (2.53 Å)