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1h32: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1h32]] 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=1H32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H32 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1h32]] 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=1H32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H32 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene></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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1h31|1h31]], [[1h33|1h33]]</div></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=1h32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h32 OCA], [https://pdbe.org/1h32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h32 RCSB], [https://www.ebi.ac.uk/pdbsum/1h32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h32 ProSAT]</span></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=1h32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h32 OCA], [https://pdbe.org/1h32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h32 RCSB], [https://www.ebi.ac.uk/pdbsum/1h32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h32 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1h32 ConSurf].
</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=1h32 ConSurf].
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== Publication Abstract from PubMed ==
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.
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<ref>PMID:12411478</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1h32" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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[[Category: Large Structures]]
[[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: Cysteine persulfide heme ligand]]
[[Category: Cytochrome c]]
[[Category: Electron transfer]]
[[Category: Soxax complex]]
[[Category: Sulfur cycle]]
[[Category: Thiosulfate oxidation]]

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