2oz1 is a 8 chain structure with sequence from Atcc 35886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
[SOXA_RHOSU] C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c and which then may be used for reductive CO(2) fixation.[1][2][3][4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
↑Cheesman MR, Little PJ, Berks BC. Novel heme ligation in a c-type cytochrome involved in thiosulfate oxidation: EPR and MCD of SoxAX from Rhodovulum sulfidophilum. Biochemistry. 2001 Sep 4;40(35):10562-9. PMID:11523998
↑Appia-Ayme C, Little PJ, Matsumoto Y, Leech AP, Berks BC. Cytochrome complex essential for photosynthetic oxidation of both thiosulfate and sulfide in Rhodovulum sulfidophilum. J Bacteriol. 2001 Oct;183(20):6107-18. PMID:11567011 doi:https://dx.doi.org/10.1128/JB.183.20.6107-6118.2001
↑Bamford VA, Bruno S, Rasmussen T, Appia-Ayme C, Cheesman MR, Berks BC, Hemmings AM. Structural basis for the oxidation of thiosulfate by a sulfur cycle enzyme. EMBO J. 2002 Nov 1;21(21):5599-610. PMID:12411478
↑Bradley JM, Marritt SJ, Kihlken MA, Haynes K, Hemmings AM, Berks BC, Cheesman MR, Butt JN. Redox and chemical activities of the hemes in the sulfur oxidation pathway enzyme SoxAX. J Biol Chem. 2012 Nov 23;287(48):40350-9. doi: 10.1074/jbc.M112.396192. Epub 2012, Oct 11. PMID:23060437 doi:https://dx.doi.org/10.1074/jbc.M112.396192
