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[[Image:1h33.gif|left|200px]]<br />
<applet load="1h33" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1h33, resolution 1.75&Aring;" />
'''OXIDISED SOXAX COMPLEX FROM RHODOVULUM SULFIDOPHILUM'''<br />


==Overview==
==Oxidised SoxAX complex from Rhodovulum sulfidophilum==
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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?12411478 (full description)]]
<StructureSection load='1h33' size='340' side='right'caption='[[1h33]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1h33]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodovulum_sulfidophilum Rhodovulum sulfidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H33 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H33 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h33 OCA], [https://pdbe.org/1h33 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h33 RCSB], [https://www.ebi.ac.uk/pdbsum/1h33 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h33 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SOXA_RHOSU 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.<ref>PMID:11523998</ref> <ref>PMID:11567011</ref> <ref>PMID:12411478</ref> <ref>PMID:23060437</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h3/1h33_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1h33 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1H33 is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Rhodovulum_sulfidophilum Rhodovulum sulfidophilum]] with HEC as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Site: HA1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H33 OCA]].
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
 
== References ==
==Reference==
<references/>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12411478 12411478]
__TOC__
[[Category: Protein complex]]
</StructureSection>
[[Category: Large Structures]]
[[Category: Rhodovulum sulfidophilum]]
[[Category: Rhodovulum sulfidophilum]]
[[Category: Appia-Ayme, C.]]
[[Category: Appia-Ayme C]]
[[Category: Bamford, V.A.]]
[[Category: Bamford VA]]
[[Category: Berks, B.C.]]
[[Category: Berks BC]]
[[Category: Bruno, S.]]
[[Category: Bruno S]]
[[Category: Cheesman, M.R.]]
[[Category: Cheesman MR]]
[[Category: Hemmings, A.M.]]
[[Category: Hemmings AM]]
[[Category: Rasmussen, T.]]
[[Category: Rasmussen T]]
[[Category: HEC]]
[[Category: cysteine persulfide heme ligand]]
[[Category: cytochrome c]]
[[Category: soxax complex]]
[[Category: sulfur cycle]]
[[Category: thiosulfate oxidation]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:29:23 2007''

Latest revision as of 14:27, 27 March 2024

Oxidised SoxAX complex from Rhodovulum sulfidophilumOxidised SoxAX complex from Rhodovulum sulfidophilum

Structural highlights

1h33 is a 2 chain structure with sequence from Rhodovulum sulfidophilum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.75Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

See Also

References

  1. ↑ 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
  2. ↑ 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:http://dx.doi.org/10.1128/JB.183.20.6107-6118.2001
  3. ↑ 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
  4. ↑ 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:http://dx.doi.org/10.1074/jbc.M112.396192

1h33, resolution 1.75Å

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