Novel domain packing in the crystal structure of a thiosulphate-oxidizing enzyme.
A key component of the oxidative biogeochemical sulphur cycle involves the utilization by bacteria of reduced inorganic sulphur compounds as electron donors to photosynthetic or respiratory electron transport chains. The SoxAX protein of the photosynthetic bacterium Rhodovulum sulfidophilum is a heterodimeric c-type cytochrome that is involved in the oxidation of thiosulphate and sulphide. The recently solved crystal structure of the SoxAX complex represents the first structurally characterized example of a productive electron transfer complex between haemoproteins where both partners adopt the c-type cytochrome fold. The packing of c-type cytochrome domains both within SoxA and at the interface between the subunits of the complex has been compared with other examples and found to be unique.
Bamford
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VA
Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK.
Berks
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BC
Hemmings
A M
AM
D001426:Bacterial Proteins; D001665:Binding Sites; D018360:Crystallography, X-Ray; D003574:Cytochrome c Group / Q000737:chemistry*; D006418:Heme / Q000378:metabolism; D008958:Models, Molecular; D010088:Oxidoreductases / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D021122:Protein Subunits / Q000737:chemistry; D012244:Rhodospirillaceae / Q000201:enzymology*
D001426:Bacterial Proteins; D003574:Cytochrome c Group; D021122:Protein Subunits; D006418:Heme; C017167:cytochrome C(551); D010088:Oxidoreductases; C090099:diheme cytochrome c