2BIW: Crystal Structure Of Apocarotenoid Cleavage Oxygenase From Synechocystis, Native Enzyme

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.
PDB ID: 2BIWDownload
MMDB ID: 33092
PDB Deposition Date: 2005/1/26
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.39  Å
Source Organism:
Similar Structures:
Biological Unit for 2BIW: monomeric; determined by author and by software (PQS)
Molecular Components in 2BIW
Label Count Molecule
Protein (1 molecule)
Apocarotenoid-cleaving Oxygenase
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB