6UWE
Crystal structure of recombinant thiocyanate dehydrogenase from Thioalkalivibrio paradoxus saturated with copper
Summary for 6UWE
| Entry DOI | 10.2210/pdb6uwe/pdb |
| Related | 6G50 6I3Q 6SJI |
| Descriptor | thiocyanate dehydrogenase, COPPER (II) ION, UNKNOWN ATOM OR ION, ... (4 entities in total) |
| Functional Keywords | thioalkalivibrio paradoxus, thiocyanate dehydrogenase, copper, oxidoreductase |
| Biological source | Thioalkalivibrio paradoxus ARh 1 |
| Total number of polymer chains | 4 |
| Total formula weight | 209639.21 |
| Authors | Shabalin, I.G.,Osipov, E.,Tikhonova, T.V.,Rakitina, T.V.,Boyko, K.M.,Popov, V.O. (deposition date: 2019-11-05, release date: 2019-11-27, Last modification date: 2023-10-11) |
| Primary citation | Tikhonova, T.V.,Sorokin, D.Y.,Hagen, W.R.,Khrenova, M.G.,Muyzer, G.,Rakitina, T.V.,Shabalin, I.G.,Trofimov, A.A.,Tsallagov, S.I.,Popov, V.O. Trinuclear copper biocatalytic center forms an active site of thiocyanate dehydrogenase. Proc.Natl.Acad.Sci.USA, 117:5280-5290, 2020 Cited by PubMed Abstract: Biocatalytic copper centers are generally involved in the activation and reduction of dioxygen, with only few exceptions known. Here we report the discovery and characterization of a previously undescribed copper center that forms the active site of a copper-containing enzyme thiocyanate dehydrogenase (suggested EC 1.8.2.7) that was purified from the haloalkaliphilic sulfur-oxidizing bacterium of the genus ubiquitous in saline alkaline soda lakes. The copper cluster is formed by three copper ions located at the corners of a near-isosceles triangle and facilitates a direct thiocyanate conversion into cyanate, elemental sulfur, and two reducing equivalents without involvement of molecular oxygen. A molecular mechanism of catalysis is suggested based on high-resolution three-dimensional structures, electron paramagnetic resonance (EPR) spectroscopy, quantum mechanics/molecular mechanics (QM/MM) simulations, kinetic studies, and the results of site-directed mutagenesis. PubMed: 32094184DOI: 10.1073/pnas.1922133117 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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