Dimeric alpha-beta barrel domains exhibit an alpha+beta sandwich fold with an antiparallel beta sheet that forms a closed barrel. These domains dimerise through the beta-sheet, and in some cases these dimers may assemble into higher oligomers. Domains with this structure are found in proteins from several different families, including bacterial actinorhodin biosynthesis monooxygenase (ActVa-Orf6), which catalyses the oxidation of an aromatic intermediate of the actinorhodin biosynthetic pathway [1]; bacterial muconalactone isomerase, a decamer composed of five dimers [2]; and the C-terminal domain of archaeal LprA, a member of the Lrp/AqsnC family of transcription regulators [3].

1. The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis. EMBO J. 22, 205-15
2. Crystal structure of muconolactone isomerase at 3.3 A resolution. J. Mol. Biol. 205, 557-71
3. Crystal structure of the Lrp-like transcriptional regulator from the archaeon Pyrococcus furiosus. EMBO J. 20, 990-7

Dimeric alpha-beta barrel domains exhibit an alpha+beta sandwich fold with an antiparallel beta s
Show more...

Download genes (select columns to include)