2C1D

Crystal structure of SoxXA from P. pantotrophus

Summary for 2C1D

• Entry DOI: 10.2210/pdb2c1d/pdb
• Descriptor: SOXA, SOXX, HEME C, ... (5 entities in total)
• Functional Keywords: sulfur oxidation, cytochrome-c-type, oxidoreductase
• Biological source: PARACOCCUS DENITRIFICANS; More
• Total number of polymer chains: 8
• Total formula weight: 182655.01

Authors

Dambe, T.,Quentmeier, A.,Rother, D.,Friedrich, C.,Scheidig, A.J. (deposition date: 2005-09-13, release date: 2005-10-06, Last modification date: 2024-10-16)

Primary citation

Dambe, T.,Quentmeier, A.,Rother, D.,Friedrich, C.,Scheidig, A.J.
Structure of the Cytochrome Complex Soxxa of Paracoccus Pantotrophus, a Heme Enzyme Initiating Chemotrophic Sulfur Oxidation.
J.Struct.Biol., 152:229-, 2005

PubMed Abstract: 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.

PubMed: 16297640
DOI: 10.1016/J.JSB.2005.09.002

Experimental method

X-RAY DIFFRACTION (1.92 Å)