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2bix
From Proteopedia
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|PDB= 2bix |SIZE=350|CAPTION= <scene name='initialview01'>2bix</scene>, resolution 2.68Å | |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> | |SITE= <scene name='pdbsite=AC1:Ote+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene> | + | |LIGAND= <scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bix OCA], [http://www.ebi.ac.uk/pdbsum/2bix PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bix RCSB]</span> | ||
}} | }} | ||
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[[Category: Ruch, S.]] | [[Category: Ruch, S.]] | ||
[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
| - | [[Category: C8E]] | ||
| - | [[Category: GOL]] | ||
[[Category: carotenoid cleavage]] | [[Category: carotenoid cleavage]] | ||
[[Category: dioxygenase]] | [[Category: dioxygenase]] | ||
| Line 36: | Line 37: | ||
[[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 Mon Mar 31 02:07:07 2008'' |
Revision as of 23:07, 30 March 2008
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| , resolution 2.68Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Mon Mar 31 02:07:07 2008
