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| | <StructureSection load='2c1d' size='340' side='right'caption='[[2c1d]], [[Resolution|resolution]] 1.92Å' scene=''> | | <StructureSection load='2c1d' size='340' side='right'caption='[[2c1d]], [[Resolution|resolution]] 1.92Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2c1d]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_17741 Atcc 17741] and [https://en.wikipedia.org/wiki/Atcc_35512 Atcc 35512]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C1D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2c1d]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans] and [https://en.wikipedia.org/wiki/Paracoccus_pantotrophus Paracoccus pantotrophus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C1D FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.92Å</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=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2c1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c1d OCA], [https://pdbe.org/2c1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c1d RCSB], [https://www.ebi.ac.uk/pdbsum/2c1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c1d 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=2c1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c1d OCA], [https://pdbe.org/2c1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c1d RCSB], [https://www.ebi.ac.uk/pdbsum/2c1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c1d ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SOXA_PARPN SOXA_PARPN]] 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 that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation.<ref>PMID:10940005</ref> <ref>PMID:16297640</ref> <ref>PMID:17547421</ref>
| + | [https://www.uniprot.org/uniprot/SOXA_PARPN SOXA_PARPN] 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 that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation.<ref>PMID:10940005</ref> <ref>PMID:16297640</ref> <ref>PMID:17547421</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 17741]] | |
| - | [[Category: Atcc 35512]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dambe, T]] | + | [[Category: Paracoccus denitrificans]] |
| - | [[Category: Friedrich, C]] | + | [[Category: Paracoccus pantotrophus]] |
| - | [[Category: Quentmeier, A]] | + | [[Category: Dambe T]] |
| - | [[Category: Rother, D]] | + | [[Category: Friedrich C]] |
| - | [[Category: Scheidig, A J]] | + | [[Category: Quentmeier A]] |
| - | [[Category: Cytochrome-c-type]] | + | [[Category: Rother D]] |
| - | [[Category: Oxidoreductase]] | + | [[Category: Scheidig AJ]] |
| - | [[Category: Sulfur oxidation]]
| + | |
| Structural highlights
Function
SOXA_PARPN 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 that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The sulfur-oxidizing enzyme system (Sox) of the chemotroph Paracoccus pantotrophus is composed of several proteins, which together oxidize hydrogen sulfide, sulfur, thiosulfate or sulfite and transfers the gained electrons to the respiratory chain. The hetero-dimeric cytochrome c complex SoxXA functions as heme enzyme and links covalently the sulfur substrate to the thiol of the cysteine-138 residue of the SoxY protein of the SoxYZ complex. Here, we report the crystal structure of the c-type cytochrome complex SoxXA. The structure could be solved by molecular replacement and refined to a resolution of 1.9A identifying the axial heme-iron coordination involving an unusual Cys-251 thiolate of heme2. Distance measurements between the three heme groups provide deeper insight into the electron transport inside SoxXA and merge in a better understanding of the initial step of the aerobic sulfur oxidation process in chemotrophic bacteria.
Structure of the cytochrome complex SoxXA of Paracoccus pantotrophus, a heme enzyme initiating chemotrophic sulfur oxidation.,Dambe T, Quentmeier A, Rother D, Friedrich C, Scheidig AJ J Struct Biol. 2005 Dec;152(3):229-34. Epub 2005 Nov 2. PMID:16297640[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Friedrich CG, Quentmeier A, Bardischewsky F, Rother D, Kraft R, Kostka S, Prinz H. Novel genes coding for lithotrophic sulfur oxidation of Paracoccus pantotrophus GB17. J Bacteriol. 2000 Sep;182(17):4677-87. PMID:10940005
- ↑ Dambe T, Quentmeier A, Rother D, Friedrich C, Scheidig AJ. Structure of the cytochrome complex SoxXA of Paracoccus pantotrophus, a heme enzyme initiating chemotrophic sulfur oxidation. J Struct Biol. 2005 Dec;152(3):229-34. Epub 2005 Nov 2. PMID:16297640 doi:10.1016/j.jsb.2005.09.002
- ↑ Reijerse EJ, Sommerhalter M, Hellwig P, Quentmeier A, Rother D, Laurich C, Bothe E, Lubitz W, Friedrich CG. The unusal redox centers of SoxXA, a novel c-type heme-enzyme essential for chemotrophic sulfur-oxidation of Paracoccus pantotrophus. Biochemistry. 2007 Jul 3;46(26):7804-10. Epub 2007 Jun 5. PMID:17547421 doi:http://dx.doi.org/10.1021/bi7003526
- ↑ Dambe T, Quentmeier A, Rother D, Friedrich C, Scheidig AJ. Structure of the cytochrome complex SoxXA of Paracoccus pantotrophus, a heme enzyme initiating chemotrophic sulfur oxidation. J Struct Biol. 2005 Dec;152(3):229-34. Epub 2005 Nov 2. PMID:16297640 doi:10.1016/j.jsb.2005.09.002
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