2bix

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Image:2bix.gif

2bix, resolution 2.68Å

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CRYSTAL STRUCTURE OF APOCAROTENOID CLEAVAGE OXYGENASE FROM SYNECHOCYSTIS, FE-FREE APOENZYME

Overview

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.

About this Structure

2BIX is a Single protein structure of sequence from Synechocystis sp. with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

The structure of a retinal-forming carotenoid oxygenase., Kloer DP, Ruch S, Al-Babili S, Beyer P, Schulz GE, Science. 2005 Apr 8;308(5719):267-9. PMID:15821095

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