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• W2337151014 abstract "The α + β barrel superfamily of the ferredoxin-like fold consists of a functionally diverse group of evolutionarily related proteins. The barrel architecture of these proteins is formed by either homo-/hetero-dimerization or duplication and fusion of ferredoxin-like domains. Several members of this superfamily bind heme in order to carry out their functions. We analyze the heme-binding sites in these proteins as well as their barrel topologies. Our comparative structural analysis of these heme-binding barrels reveals two distinct modes of packing of the ferredoxin-like domains to constitute the α + β barrel, which is typified by the Type-1/IsdG-like and Type-2/OxdA-like proteins, respectively. We examine the heme-binding pockets and explore the versatility of the α + β barrels ability to accommodate heme or heme-related moieties, such as siroheme, in at least three different sites, namely, the mode seen in IsdG/OxdA, Cld/DyP/EfeB/HemQ and siroheme decarboxylase barrels. Our study offers insights into the plausible evolutionary relationships between the two distinct barrel packing topologies and relate the observed heme-binding sites to these topologies." @default.
• W2337151014 created "2016-06-24" @default.
• W2337151014 creator A5017697005 @default.
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• W2337151014 date "2016-04-18" @default.
• W2337151014 modified "2023-10-16" @default.
• W2337151014 title "Evolutionary relationships between heme-binding ferredoxin α + β barrels" @default.
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• W2337151014 doi "https://doi.org/10.1186/s12859-016-1033-6" @default.
• W2337151014 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4835899" @default.
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• W2337151014 hasPublicationYear "2016" @default.
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