The structure of a retinal-forming carotenoid oxygenase

Daniel P. Kloer; Sandra Ruch; Salim Al-Babili; Peter Beyer; Georg E. Schulz

doi:10.1126/science.1108965

The structure of a retinal-forming carotenoid oxygenase

Daniel P. Kloer, Sandra Ruch, Salim Al-Babili, Peter Beyer, Georg E. Schulz^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

229 Scopus citations

Abstract

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 β-propeller chain fold covered by a dome formed by six large loops. The Fe²⁺ 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 Fe²⁺ and cleaved by oxygen.

Original language	English (US)
Pages (from-to)	267-269
Number of pages	3
Journal	SCIENCE
Volume	308
Issue number	5719
DOIs	https://doi.org/10.1126/science.1108965
State	Published - Apr 8 2005
Externally published	Yes

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title = "The structure of a retinal-forming carotenoid oxygenase",

abstract = "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 β-propeller chain fold covered by a dome formed by six large loops. The Fe2+ 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 Fe2+ and cleaved by oxygen.",

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AU - Al-Babili, Salim

AU - Beyer, Peter

AU - Schulz, Georg E.

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N2 - 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 β-propeller chain fold covered by a dome formed by six large loops. The Fe2+ 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 Fe2+ and cleaved by oxygen.

AB - 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 β-propeller chain fold covered by a dome formed by six large loops. The Fe2+ 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 Fe2+ and cleaved by oxygen.

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The structure of a retinal-forming carotenoid oxygenase

Abstract

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