Related Experiment Videos
Cupins: the most functionally diverse protein superfamily?
Jim M Dunwell1, Alan Purvis, Sawsan Khuri
1The BioCentre, School of Plant Sciences, The University of Reading, Whiteknights, Reading, RG6 6AS, UK.
Phytochemistry
|December 31, 2003
Summary
The cupin superfamily encompasses diverse proteins with a conserved beta-barrel fold. This review highlights 2-oxyglutarate-Fe(2+) dependent dioxygenases as the largest subset, involved in numerous biochemical reactions, including plant growth.
Area of Science:
- Biochemistry
- Structural Biology
- Genomics
Background:
- The cupin superfamily is defined by a conserved beta-barrel fold, originally identified in plant proteins.
- Previous studies recognized 18 functional classes of cupins, including enzymes and transcription factors.
- Recent advances reveal a vast diversity within this protein family.
Purpose of the Study:
- To review the structural and functional diversity of the cupin superfamily.
- To highlight the 2-oxyglutarate-Fe(2+) dependent dioxygenases as the largest cupin subclass.
- To discuss the role of various metal cofactors in cupin enzymatic activity.
Main Methods:
- Comparative genomics analysis
- 3-D structure resolution
- Literature review of biochemical functions
Main Results:
- The 2-oxyglutarate-Fe(2+) dependent dioxygenases represent the largest subset of cupins.
- This subclass catalyzes a wide range of biochemical reactions (50-100), including those crucial for plant development.
- Cupins utilize diverse metal cofactors (Fe, Cu, Zn, Co, Ni, Mn) for distinct enzymatic activities.
Conclusions:
- The cupin superfamily is exceptionally diverse in structure and function.
- Metal-dependent dioxygenases are a major functional group within cupins.
- Cupins play significant roles in various biological processes across different organisms.