2biw
From Proteopedia
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|PDB= 2biw |SIZE=350|CAPTION= <scene name='initialview01'>2biw</scene>, resolution 2.39Å | |PDB= 2biw |SIZE=350|CAPTION= <scene name='initialview01'>2biw</scene>, resolution 2.39Å | ||
|SITE= <scene name='pdbsite=AC1:Fe+Binding+Site+For+Chain+D'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Fe+Binding+Site+For+Chain+D'>AC1</scene> | ||
- | |LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> and <scene name='pdbligand=3ON:(3R)-3-HYDROXY-8 | + | |LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> and <scene name='pdbligand=3ON:(3R)-3-HYDROXY-8'-APOCAROTENOL'>3ON</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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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 Sun Mar 23 14:45:23 2008'' |
Revision as of 12:45, 23 March 2008
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, resolution 2.39Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
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
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