1h33

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{{STRUCTURE_1h33| PDB=1h33 | SCENE= }}
{{STRUCTURE_1h33| PDB=1h33 | SCENE= }}
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'''OXIDISED SOXAX COMPLEX FROM RHODOVULUM SULFIDOPHILUM'''
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===OXIDISED SOXAX COMPLEX FROM RHODOVULUM SULFIDOPHILUM===
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==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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{{ABSTRACT_PUBMED_12411478}}
==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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Revision as of 03:32, 1 July 2008

Image:1h33.png

Template:STRUCTURE 1h33

OXIDISED SOXAX COMPLEX FROM RHODOVULUM SULFIDOPHILUM

Template:ABSTRACT PUBMED 12411478

About this Structure

1H33 is a Protein complex structure of sequences from Rhodovulum sulfidophilum. Full crystallographic information is available from OCA.

Reference

Structural basis for the oxidation of thiosulfate by a sulfur cycle enzyme., Bamford VA, Bruno S, Rasmussen T, Appia-Ayme C, Cheesman MR, Berks BC, Hemmings AM, EMBO J. 2002 Nov 1;21(21):5599-610. PMID:12411478

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