2bix: Difference between revisions
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[[Image:2bix.gif|left|200px]] | [[Image:2bix.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF APOCAROTENOID CLEAVAGE OXYGENASE FROM SYNECHOCYSTIS, FE-FREE APOENZYME''' | {{Structure | ||
|PDB= 2bix |SIZE=350|CAPTION= <scene name='initialview01'>2bix</scene>, resolution 2.68Å | |||
|SITE= <scene name='pdbsite=AC1:Ote+Binding+Site+For+Chain+B'>AC1</scene> | |||
|LIGAND= <scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF APOCAROTENOID CLEAVAGE OXYGENASE FROM SYNECHOCYSTIS, FE-FREE APOENZYME''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2BIX is a [ | 2BIX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BIX OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15821095 15821095] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Synechocystis sp.]] | [[Category: Synechocystis sp.]] | ||
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[[Category: retinal formation]] | [[Category: retinal formation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:02:38 2008'' | ||
Revision as of 14:02, 20 March 2008
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| 2bix, resolution 2.68Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | C8E and GOL | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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.. 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 Mar 20 16:02:38 2008
