Evolution of functional diversity in the cupin superfamily

• Published in: Trends in Biochemical Sciences 2001-12, Vol.26 (12), p.740-746
• Main Authors: Dunwell, Jim M, Culham, Alastair, Carter, Carol E, Sosa-Aguirre, Carlos R, Goodenough, Peter W
• Format: Article
• Language: English
• Subjects: Amino Acid Motifs; Amino Acid Sequence; Animals; auxin binding protein; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - physiology; Binding Sites; CENP-C; dioxygenase; dTDP-L-rhamnose; Evolution, Molecular; Genetic Variation; germin; Molecular Sequence Data; oxalate oxidase; phosphomannose isomerase; Phylogeny; pirin; Plant Proteins - chemistry; Plant Proteins - genetics; Plant Proteins - physiology; Protein Structure, Tertiary; Sequence Alignment; Transcription Factors - chemistry; Transcription Factors - genetics; Transcription Factors - physiology
• ISSN: 0968-0004; 1362-4326
• DOI: 10.1016/S0968-0004(01)01981-8

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 β-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. This molecular archaeology review describes the discovery of the early ancestors of the plant proteins that now make up a major part of the human diet.