In molecular biology dimeric alpha beta barrel domain (Dim_A_B_barrel) is a protein structural motif found in proteins with a ferredoxin-like fold.
Structure Pairs of these proteins assemble into a beta barrel structure. Dimeric α-β barrel domains exhibit an α+β sandwich fold with an antiparallel β-sheet that forms a closed barrel. These domains dimerise through the β-sheet, and in some cases these dimers may assemble into higher oligomers.
Function The function of this barrel is quite varied, indicating versatility in its biological roles.
Examples 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 Bacterial muconalactone isomerase, a decamer composed of five dimers The C-terminal domain of archaeal LprA, a member of the Lrp/AqsnC family of transcription regulators
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