1h33: Difference between revisions

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[[Image:1h33.jpg|left|200px]]
{{Seed}}
[[Image:1h33.png|left|200px]]


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{{STRUCTURE_1h33|  PDB=1h33  |  SCENE=  }}  
{{STRUCTURE_1h33|  PDB=1h33  |  SCENE=  }}  


'''OXIDISED SOXAX COMPLEX FROM RHODOVULUM SULFIDOPHILUM'''
===OXIDISED SOXAX COMPLEX FROM RHODOVULUM SULFIDOPHILUM===




==Overview==
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Reduced inorganic sulfur compounds are utilized by many bacteria as electron donors to photosynthetic or respiratory electron transport chains. This metabolism is a key component of the biogeochemical sulfur cycle. The SoxAX protein is a heterodimeric c-type cytochrome involved in thiosulfate oxidation. The crystal structures of SoxAX from the photosynthetic bacterium Rhodovulum sulfidophilum have been solved at 1.75 A resolution in the oxidized state and at 1.5 A resolution in the dithionite-reduced state, providing the first structural insights into the enzymatic oxidation of thiosulfate. The SoxAX active site contains a haem with unprecedented cysteine persulfide (cysteine sulfane) coordination. This unusual post-translational modification is also seen in sulfurtransferases such as rhodanese. Intriguingly, this enzyme shares further active site characteristics with SoxAX such as an adjacent conserved arginine residue and a strongly positive electrostatic potential. These similarities have allowed us to suggest a catalytic mechanism for enzymatic thiosulfate oxidation. The atomic coordinates and experimental structure factors have been deposited in the PDB with the accession codes 1H31, 1H32 and 1H33.
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==About this Structure==
==About this Structure==
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[[Category: Sulfur cycle]]
[[Category: Sulfur cycle]]
[[Category: Thiosulfate oxidation]]
[[Category: Thiosulfate oxidation]]
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