Structural highlights
Publication Abstract from PubMedThe 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. Modular evolution and the origins of symmetry: reconstruction of a three-fold symmetric globular protein.,Broom A, Doxey AC, Lobsanov YD, Berthin LG, Rose DR, Howell PL, McConkey BJ, Meiering EM Structure. 2012 Jan 11;20(1):161-71. Epub 2011 Dec 15. PMID:22178248[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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