2biw
From Proteopedia
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[[Category: retinal formation]] | [[Category: retinal formation]] | ||
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Revision as of 14:34, 30 October 2007
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CRYSTAL STRUCTURE OF APOCAROTENOID CLEAVAGE OXYGENASE FROM SYNECHOCYSTIS, NATIVE ENZYME
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
2BIW is a [Single protein] structure of sequence from [Synechocystis sp.] with FE and 3ON as [ligands]. The following page contains interesting information on the relation of 2BIW with [Carotenoid Oxygenase]. Structure known Active Site: AC1. 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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