The structure of a retinal-forming carotenoid oxygenase

被引：211

作者：

Kloer, DP

Ruch, S

Al-Babili, S

Beyer, P

Schulz, GE

机构：

[1] Univ Freiburg, Inst Organ Chem & Biochem, D-79104 Freiburg, Germany

[2] Univ Freiburg, Inst Biol 2, D-79104 Freiburg, Germany

来源：

SCIENCE | 2005年 / 308卷 / 5719期

关键词：

D O I：

10.1126/science.1108965

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 Fe2+-4-His arrangement at the axis of a seven-bladed beta-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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收藏

页码：267 / 269

页数：3

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