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Evolution of functional diversity in the cupin superfamily

By Jim M. Dunwell, Alastair Culham, Carol E. Carter, Carlos Sosa-Aguirre and Peter W. Goodenough

Abstract

The cupin superfamily of proteins is among the most functionally diverse of any described to date. It was named on the basis of the conserved beta-barrel fold ('cupa' is the Latin term for a small barrel), and comprises both enzymatic and non-enzymatic members, which have either one or two cupin domains. Within the conserved tertiary structure, the variety of biochemical function is provided by minor variation of the residues in the active site and the identity of the bound metal ion. This review discusses the advantages of this particular scaffold and provides an evolutionary analysis of 18 different subclasses within the cupin superfamily

Publisher: International Union of Biochemistry and Molecular Biology
Year: 2001
OAI identifier: oai:centaur.reading.ac.uk:7947
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  • http://dx.doi.org/10.1016/S096... (external link)
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