3PG0: Crystal structure of designed 3-fold symmetric protein, ThreeFoil

The high frequency of internal structural symmetry in common protein folds is presumed to reflect their evolutionary origins from the repetition and fusion of ancient peptide modules, but little is known about the primary sequence and physical determinants of this process. Unexpectedly, a sequence and structural analysis of symmetric subdomain modules within an abundant and ancient globular fold, the beta-trefoil, reveals that modular evolution is not simply a relic of the ancient past, but is an ongoing and recurring mechanism for regenerating symmetry, having occurred independently in numerous existing beta-trefoil proteins. We performed a computational reconstruction of a beta-trefoil subdomain module and repeated it to form a newly three-fold symmetric globular protein, ThreeFoil. In addition to its near perfect structural identity between symmetric modules, ThreeFoil is highly soluble, performs multivalent carbohydrate binding, and has remarkably high thermal stability. These findings have far-reaching implications for understanding the evolution and design of proteins via subdomain modules.
PDB ID: 3PG0Download
MMDB ID: 95857
PDB Deposition Date: 2010/10/29
Updated in MMDB: 2011/12
Experimental Method:
x-ray diffraction
Resolution: 1.62  Å
Source Organism:
Similar Structures:
Biological Unit for 3PG0: monomeric; determined by author and by software (PISA)
Molecular Components in 3PG0
Label Count Molecule
Protein (1 molecule)
Molecule annotation
Chemicals (6 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB