On the evolution of alternate core packing in eightfold beta/alpha-barrels.
作者： Andrew R.C. Raine , Nigel S. Scrutton , F. Scott Mathews
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摘要: Two sequence-related subfamilies of flavin-binding beta/alpha-barrels have been identified (the type I and II proteins) that differ in the nature residue packing core barrel domain. Similar observed differences internal amino acid side chains previously used to argue these domains evolved convergently toward a stable structural framework. Using alignments proteins, we demonstrate simple genetic alterations may be responsible for switching side-chain beta/alpha-barrels. The implication is 2 classes beta/alpha-barrel cores can arise divergently from an ancestral framework convergent evolution fold need not invoked account emergence core.
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