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Science 8 April 2005: Vol. 308. no. 5719, pp. 267 - 269 DOI: 10.1126/science.1108965
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Reports
The Structure of a Retinal-Forming Carotenoid Oxygenase
Daniel P. Kloer,1
Sandra Ruch,2
Salim Al-Babili,2
Peter Beyer,2
Georg E. Schulz1*
Enzymes that produce retinal and related apocarotenoids constitute a sequence- and thus structure-related family, a member of which was analyzed by x-ray diffraction. This member is an oxygenase and contains an Fe 2+-4-His arrangement at the axis of a seven-bladed ß-propeller chain fold covered by a dome formed by six large loops. The Fe 2+ is accessible through a long nonpolar tunnel that holds a carotenoid derivative in one of the crystals. On binding, three consecutive double bonds of this carotenoid changed from a straight all-trans to a cranked cis-trans-cis conformation. The remaining trans bond is located at the dioxygen-ligated Fe 2+ and cleaved by oxygen.
1 Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Albertstrasse 21, 79104 Freiburg im Breisgau, Germany.
2 Institut für Biologie II, Albert-Ludwigs-Universität, Schänzlestrasse 1, 79104 Freiburg im Breisgau, Germany.
* To whom correspondence should be addressed. E-mail: georg.schulz{at}ocbc.uni-freiburg.de
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