7O9U

Solution structure of oxidized cytochrome c552 from Thioalkalivibrio paradoxus

Replaces:  6TK0

Summary for 7O9U

• Entry DOI: 10.2210/pdb7o9u/pdb
• NMR Information: BMRB: 34460,34618
• Descriptor: Cytochrome c552, HEME C (2 entities in total)
• Functional Keywords: thiocyanate dehydrogenase electron acceptor, cytochrome c552, class i cytochrome c, hemeprotein, periplasmic, electron transport
• Biological source: Thioalkalivibrio paradoxus ARh 1
• Total number of polymer chains: 1
• Total formula weight: 17355.57

Authors

Britikov, V.V.,Britikova, E.V.,Altukhov, D.A.,Timofeev, V.I.,Dergousova, N.I.,Rakitina, T.V.,Tikhonova, T.V.,Usanov, S.A.,Popov, V.O.,Bocharov, E.V. (deposition date: 2021-04-17, release date: 2021-05-05, Last modification date: 2024-11-20)

Primary citation

Britikov, V.V.,Bocharov, E.V.,Britikova, E.V.,Dergousova, N.I.,Kulikova, O.G.,Solovieva, A.Y.,Shipkov, N.S.,Varfolomeeva, L.A.,Tikhonova, T.V.,Timofeev, V.I.,Shtykova, E.V.,Altukhov, D.A.,Usanov, S.A.,Arseniev, A.S.,Rakitina, T.V.,Popov, V.O.
Unusual Cytochrome c 552 from Thioalkalivibrio paradoxus : Solution NMR Structure and Interaction with Thiocyanate Dehydrogenase.
Int J Mol Sci, 23:-, 2022

PubMed Abstract: The search of a putative physiological electron acceptor for thiocyanate dehydrogenase (TcDH) newly discovered in the thiocyanate-oxidizing bacteria revealed an unusually large, single-heme cytochrome (CytC552), which was co-purified with TcDH from the periplasm. Recombinant CytC552, produced in as a mature protein without a signal peptide, has spectral properties similar to the endogenous protein and serves as an in vitro electron acceptor in the TcDH-catalyzed reaction. The CytC552 structure determined by NMR spectroscopy reveals significant differences compared to those of the typical class I bacterial cytochromes : a high solvent accessible surface area for the heme group and so-called "intrinsically disordered" nature of the histidine-rich N- and C-terminal regions. Comparison of the signal splitting in the heteronuclear NMR spectra of oxidized, reduced, and TcDH-bound CytC552 reveals the heme axial methionine fluxionality. The TcDH binding site on the CytC552 surface was mapped using NMR chemical shift perturbations. Putative TcDH-CytC552 complexes were reconstructed by the information-driven docking approach and used for the analysis of effective electron transfer pathways. The best pathway includes the electron hopping through His528 and Tyr164 of TcDH, and His83 of CytC552 to the heme group in accordance with pH-dependence of TcDH activity with CytC552.

PubMed: 36077365
DOI: 10.3390/ijms23179969

Experimental method

SOLUTION NMR