2biw
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Enzymes that produce retinal and related apocarotenoids constitute a | + | 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== | ==About this Structure== | ||
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[[Category: Al-Babili, S.]] | [[Category: Al-Babili, S.]] | ||
[[Category: Beyer, P.]] | [[Category: Beyer, P.]] | ||
| - | [[Category: Kloer, D | + | [[Category: Kloer, D P.]] |
[[Category: Ruch, S.]] | [[Category: Ruch, S.]] | ||
| - | [[Category: Schulz, G | + | [[Category: Schulz, G E.]] |
[[Category: 3ON]] | [[Category: 3ON]] | ||
[[Category: FE]] | [[Category: FE]] | ||
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[[Category: retinal formation]] | [[Category: retinal formation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:38:19 2008'' |
Revision as of 14:38, 21 February 2008
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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 and as ligands. The following page contains interesting information on the relation of 2BIW with [Carotenoid Oxygenase]. 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
Page seeded by OCA on Thu Feb 21 16:38:19 2008
