2XTS

Crystal Structure of the Sulfane Dehydrogenase SoxCD from Paracoccus pantotrophus

Summary for 2XTS

• Entry DOI: 10.2210/pdb2xts/pdb
• Related: 1WQ0
• Descriptor: SULFITE DEHYDROGENASE, CYTOCHROME, PHOSPHONIC ACIDMONO-(2-AMINO-5,6-DIMERCAPTO-4-OXO-3,7,8A,9,10,10A-HEXAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-7-YLMETHYL)ESTER, ... (9 entities in total)
• Functional Keywords: oxidoreductase-electron transport complex, sox system, sulfane oxidation, molybdenum cofactor, heme, electron transfer, oxidoreductase/electron transport
• Biological source: PARACOCCUS PANTOTROPHUS; More
• Total number of polymer chains: 4
• Total formula weight: 134254.98

Authors

Zander, U.,Faust, A.,Klink, B.U.,de Sanctis, D.,Panjikar, S.,Quentmeier, A.,Bardischewski, F.,Friedrich, C.G.,Scheidig, A.J. (deposition date: 2010-10-12, release date: 2010-12-08, Last modification date: 2024-11-20)

Primary citation

Zander, U.,Faust, A.,Klink, B.U.,De Sanctis, D.,Panjikar, S.,Quentmeier, A.,Bardischewsky, F.,Friedrich, C.G.,Scheidig, A.J.
Structural Basis for the Oxidation of Protein-Bound Sulfur by the Sulfur Cycle Molybdohemo-Enzyme Sulfane Dehydrogenase Soxcd.
J.Biol.Chem., 286:8349-, 2011

PubMed Abstract: The sulfur cycle enzyme sulfane dehydrogenase SoxCD is an essential component of the sulfur oxidation (Sox) enzyme system of Paracoccus pantotrophus. SoxCD catalyzes a six-electron oxidation reaction within the Sox cycle. SoxCD is an α(2)β(2) heterotetrameric complex of the molybdenum cofactor-containing SoxC protein and the diheme c-type cytochrome SoxD with the heme domains D(1) and D(2). SoxCD(1) misses the heme-2 domain D(2) and is catalytically as active as SoxCD. The crystal structure of SoxCD(1) was solved at 1.33 Å. The substrate of SoxCD is the outer (sulfane) sulfur of Cys-110-persulfide located at the C-terminal peptide swinging arm of SoxY of the SoxYZ carrier complex. The SoxCD(1) substrate funnel toward the molybdopterin is narrow and partially shielded by side-chain residues of SoxD(1). For access of the sulfane-sulfur of SoxY-Cys-110 persulfide we propose that (i) the blockage by SoxD-Arg-98 is opened via interaction with the C terminus of SoxY and (ii) the C-terminal peptide VTIGGCGG of SoxY provides interactions with the entrance path such that the cysteine-bound persulfide is optimally positioned near the molybdenum atom. The subsequent oxidation reactions of the sulfane-sulfur are initiated by the nucleophilic attack of the persulfide anion on the molybdenum atom that is, in turn, reduced. The close proximity of heme-1 to the molybdopterin allows easy acceptance of the electrons. Because SoxYZ, SoxXA, and SoxB are already structurally characterized, with SoxCD(1) the structures of all key enzymes of the Sox cycle are known with atomic resolution.

PubMed: 21147779
DOI: 10.1074/JBC.M110.193631

Experimental method

X-RAY DIFFRACTION (1.33 Å)