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2biw
From Proteopedia
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[[Image:2biw.gif|left|200px]] | [[Image:2biw.gif|left|200px]] | ||
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'''CRYSTAL STRUCTURE OF APOCAROTENOID CLEAVAGE OXYGENASE FROM SYNECHOCYSTIS, NATIVE ENZYME''' | '''CRYSTAL STRUCTURE OF APOCAROTENOID CLEAVAGE OXYGENASE FROM SYNECHOCYSTIS, NATIVE ENZYME''' | ||
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[[Category: Ruch, S.]] | [[Category: Ruch, S.]] | ||
[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
| - | [[Category: | + | [[Category: Dioxygenase]] |
| - | [[Category: | + | [[Category: Oxidoreductase]] |
| - | [[Category: | + | [[Category: Oxygenase,non-heme iron,carotenoid cleavage,retinal formation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:21:12 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:21, 3 May 2008
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.. The following page contains interesting information on the relation of 2BIW with [Carotenoid Oxygenase]. 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 Page seeded by OCA on Sat May 3 20:21:12 2008
