5N1T
Crystal structure of complex between flavocytochrome c and copper chaperone CopC from T. paradoxus
Summary for 5N1T
| Entry DOI | 10.2210/pdb5n1t/pdb |
| Descriptor | flavin-binding subunit of sulfide dehydrogenase, Cytochrome C, CopC, ... (8 entities in total) |
| Functional Keywords | copper chaperone, sulfide reductase, periplasm, protein complex, oxidoreductase |
| Biological source | Thioalkalivibrio paradoxus ARh 1 More |
| Total number of polymer chains | 4 |
| Total formula weight | 92324.90 |
| Authors | Osipov, E.M.,Lilina, A.V.,Tikhonova, T.V.,Tsallagov, S.I.,Popov, V.O. (deposition date: 2017-02-06, release date: 2018-02-28, Last modification date: 2025-10-01) |
| Primary citation | Osipov, E.M.,Lilina, A.V.,Tsallagov, S.I.,Safonova, T.N.,Sorokin, D.Y.,Tikhonova, T.V.,Popov, V.O. Structure of the flavocytochrome c sulfide dehydrogenase associated with the copper-binding protein CopC from the haloalkaliphilic sulfur-oxidizing bacterium Thioalkalivibrio paradoxusARh 1. Acta Crystallogr D Struct Biol, 74:632-642, 2018 Cited by PubMed Abstract: Flavocytochrome c sulfide dehydrogenase from Thioalkalivibrio paradoxus (TpFCC) is a heterodimeric protein consisting of flavin- and monohaem c-binding subunits. TpFCC was co-purified and co-crystallized with the dimeric copper-binding protein TpCopC. The structure of the TpFCC-(TpCopC) complex was determined by X-ray diffraction at 2.6 Å resolution. The flavin-binding subunit of TpFCC is structurally similar to those determined previously, and the structure of the haem-binding subunit is similar to that of the N-terminal domain of dihaem FCCs. According to classification based on amino-acid sequence, TpCopC belongs to a high-affinity CopC subfamily characterized by the presence of a conserved His1-Xxx-His3 motif at the N-terminus. Apparently, a unique α-helix which is present in each monomer of TpCopC at the interface with TpFCC plays a key role in complex formation. The structure of the copper-binding site in TpCopC is similar to those in other known CopC structures. His3 is not involved in binding to the copper ion and is 6-7 Å away from this ion. Therefore, the His1-Xxx-His3 motif cannot be considered to be a key factor in the high affinity of CopC for copper(II) ions. It is suggested that the TpFCC-(TpCopC) heterotetramer may be a component of a large periplasmic complex that is responsible for thiocyanate metabolism. PubMed: 29968673DOI: 10.1107/S2059798318005648 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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