Article citationsMore>>
Adams, P.D., Afonine, P.V., Bunkóczi, G., Chen, V.B., Davis, I.W., Echols, N., Headd, J.J., Hung, L.-W., Kapral, G.J., Grosse-Kunstleve, R.W., McCoy, A.J., Moriarty, N.W., Oeffner, R., Read, R.J., Richardson, D.C., Richardson, J.S., Terwilliger, T.C. and Zwart, P.H. (2010) PHENIX: A Comprehensive Python-Based System for Macromolecular Structure Solution. Acta Crystallographica, D66, 213-221.
http://dx.doi.org/10.1107/s0907444909052925
has been cited by the following article:
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TITLE:
Subunit Arrangement of a 2-Ketoisovalerate Ferredoxin Oxidoreductase from Thermococcus profundus Revealed by a Low Resolution X-Ray Analysis
AUTHORS:
Yukiko Ozawa, Yasufumi Umena, Takeo Imai, Yukio Morimoto
KEYWORDS:
Oxidoreductase, X-Ray Analysis, Iron-Sulfur Cluster
JOURNAL NAME:
Advances in Enzyme Research,
Vol.3 No.3,
September
8,
2015
ABSTRACT: 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 Å, c = 221.07 Å. Diffraction images were processed to a resolution of 3.0 Å. The data collected so far indicate the approximate molecular boundaries and a partial main-chain trace of the enzyme.
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