2BIX

Crystal structure of apocarotenoid cleavage oxygenase from Synechocystis, Fe-free apoenzyme

Summary for 2BIX

• Entry DOI: 10.2210/pdb2bix/pdb
• Related: 2BIW
• Descriptor: APOCAROTENOID-CLEAVING OXYGENASE, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, GLYCEROL, ... (4 entities in total)
• Functional Keywords: oxygenase, non-heme iron, carotenoid cleavage, retinal formation, oxidoreductase, dioxygenase
• Biological source: SYNECHOCYSTIS SP.
• Total number of polymer chains: 2
• Total formula weight: 109485.45

Authors

Kloer, D.P.,Ruch, S.,Al-Babili, S.,Beyer, P.,Schulz, G.E. (deposition date: 2005-01-26, release date: 2005-04-14, Last modification date: 2024-05-08)

Primary citation

Kloer, D.P.,Ruch, S.,Al-Babili, S.,Beyer, P.,Schulz, G.E.
The Structure of a Retinal-Forming Carotenoid Oxygenase
Science, 308:267-, 2005

PubMed Abstract: 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.

PubMed: 15821095
DOI: 10.1126/SCIENCE.1108965

Experimental method

X-RAY DIFFRACTION (2.68 Å)