2bix
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 2BIX is a | + | 2BIX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.] with C8E and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BIX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: retinal formation]] | [[Category: retinal formation]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:21:22 2007'' |
Revision as of 13:16, 5 November 2007
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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 C8E and GOL as ligands. 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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