2c1d
From Proteopedia
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|PDB= 2c1d |SIZE=350|CAPTION= <scene name='initialview01'>2c1d</scene>, resolution 1.92Å | |PDB= 2c1d |SIZE=350|CAPTION= <scene name='initialview01'>2c1d</scene>, resolution 1.92Å | ||
|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c1d OCA], [http://www.ebi.ac.uk/pdbsum/2c1d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c1d RCSB]</span> | ||
}} | }} | ||
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[[Category: Rother, D.]] | [[Category: Rother, D.]] | ||
[[Category: Scheidig, A J.]] | [[Category: Scheidig, A J.]] | ||
| - | [[Category: HEC]] | ||
| - | [[Category: ZN]] | ||
[[Category: cytochrome-c-type]] | [[Category: cytochrome-c-type]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
[[Category: sulfur oxidation]] | [[Category: sulfur oxidation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:14:50 2008'' |
Revision as of 23:14, 30 March 2008
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| , resolution 1.92Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF SOXXA FROM P. PANTOTROPHUS
Overview
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.
About this Structure
2C1D is a Protein complex structure of sequences from Paracoccus denitrificans and Paracoccus pantotrophus. Full crystallographic information is available from OCA.
Reference
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
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