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Protein Science, Vol 3, Issue 10 1889-1892, Copyright © 1994 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

On the evolution of alternate core packing in eightfold {beta}/{alpha}-barrels

ARC. RAINE, N. S. SCRUTTON and F. S. MATHEWS
Centre for Molecular Recognition, Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, United Kingdom

Two sequence-related subfamilies of flavin-binding {beta}/{alpha}-barrels have been identified (the type I and type II proteins) that differ in the nature of residue packing in the core of the barrel domain. Similar observed differences in the packing of internal amino acid side chains in {beta}/{alpha}-barrels have previously been used to argue that these domains have evolved convergently toward a stable structural framework. Using structural alignments of flavin-binding barrel proteins, we demonstrate that simple genetic alterations may be responsible for switching the nature of side-chain packing observed in {beta}/{alpha}-barrels. The implication is that the 2 structural classes of {beta}/{alpha}-barrel cores can arise divergently from an ancestral barrel framework and that convergent evolution to a stable fold need not be invoked to account for the emergence of 2 classes of {beta}/{alpha}-barrel core.
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[Abstract] [Full Text] [PDF]


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