5N1T

Crystal structure of complex between flavocytochrome c and copper chaperone CopC from T. paradoxus

5N1T の概要

• エントリーDOI: 10.2210/pdb5n1t/pdb
• 分子名称: flavin-binding subunit of sulfide dehydrogenase, Cytochrome C, CopC, ... (8 entities in total)
• 機能のキーワード: copper chaperone, sulfide reductase, periplasm, protein complex, oxidoreductase
• 由来する生物種: Thioalkalivibrio paradoxus ARh 1; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 92324.90

構造登録者

Osipov, E.M.,Lilina, A.V.,Tikhonova, T.V.,Tsallagov, S.I.,Popov, V.O. (登録日: 2017-02-06, 公開日: 2018-02-28, 最終更新日: 2025-10-01)

主引用文献

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

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: 29968673
DOI: 10.1107/S2059798318005648

実験手法

X-RAY DIFFRACTION (2.6 Å)