Subunit Arrangement of a 2-Ketoisovalerate Ferredoxin Oxidoreductase from Thermococcus profundus Revealed by a Low Resolution X-Ray Analysis
Autor: | Yasufumi Umena, Takeo Imai, Yukio Morimoto, Yukiko Ozawa |
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Rok vydání: | 2015 |
Předmět: |
chemistry.chemical_classification
biology Protein subunit Iron–sulfur cluster biology.organism_classification Cofactor Hyperthermophile Crystallography chemistry.chemical_compound chemistry Oxidoreductase Thermococcus profundus biology.protein General Materials Science Ferredoxin Oxidative decarboxylation |
Zdroj: | Advances in Enzyme Research. :75-80 |
ISSN: | 2328-4854 2328-4846 |
Popis: | 2-ketoisovalerate ferredoxin oxidoreductase (VOR) is a key enzyme in hyperthermophiles catalyzing the coenzyme A-dependent oxidative decarboxylation of aliphatic amino acid-derived 2-keto acids. The enzyme purified under anaerobic conditions from a hyperthermophilic archaeon, Thermococcus profundus, is a hetero-octamer (αβγδ)2 consisting of four different subunits, α = 45 kDa, β = 31 kDa, γ = 22 kDa and δ = 13 kDa, respectively, and it has three [4Fe-4S] clusters per αβγδ-protomer, similar to other ferredoxin oxidoreductases. In the present study, the native enzyme was purified from this strain and crystallized to give rod-like crystals that were suitable for X-ray diffraction experiments. The crystals belonged to space group P41212, with unit-cell parameters a = b = 136.20 A, c = 221.07 A. Diffraction images were processed to a resolution of 3.0 A. The data collected so far indicate the approximate molecular boundaries and a partial main-chain trace of the enzyme. |
Databáze: | OpenAIRE |
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