Subunit Arrangement of a 2-Ketoisovalerate Ferredoxin Oxidoreductase from Thermococcus profundus Revealed by a Low Resolution X-Ray Analysis
Subunit Arrangement of a 2-Ketoisovalerate Ferredoxin Oxidoreductase from Thermococcus profundus Revealed by a Low Resolution X-Ray Analysis作者机构：Department of Life Science and Graduate School of Life Science Rikkyo (St. Paul’s) University Tokyo Japan Photosynthesis Research Center Okayama University Okayama Japan Research Reactor Institute Kyoto University Osaka Japan
出 版 物：《Advances in Enzyme Research》 (酶研究进展（英文）)
年 卷 期：2015年第3卷第3期
页 面：75-80页
学科分类：1002[医学-临床医学] 100214[医学-肿瘤学] 10[医学]
主 题：Oxidoreductase X-Ray Analysis Iron-Sulfur Cluster
摘 要：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 ?, c = 221.07 ?. Diffraction images were processed to a resolution of 3.0 ?. The data collected so far indicate the approximate molecular boundaries and a partial main-chain trace of the enzyme.
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