3O4C

Crystal structure of Symfoil-4V: de novo designed beta-trefoil architecture with symmetric primary structure

Summary for 3O4C

• Entry DOI: 10.2210/pdb3o4c/pdb
• Related: 1JQZ 3O3Q 3O49 3O4A 3O4B 3O4D 3O4E
• Descriptor: de novo designed beta-trefoil architecture with symmetric primary structure, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, SULFATE ION, ... (5 entities in total)
• Functional Keywords: beta-trefoil, de novo protein
• Biological source: synthetic construct (artificial gene)
• Total number of polymer chains: 1
• Total formula weight: 16254.48

Authors

Lee, J.,Blaber, M. (deposition date: 2010-07-26, release date: 2010-12-22, Last modification date: 2024-02-21)

Primary citation

Lee, J.,Blaber, M.
Experimental support for the evolution of symmetric protein architecture from a simple peptide motif.
Proc.Natl.Acad.Sci.USA, 108:126-130, 2011

PubMed Abstract: The majority of protein architectures exhibit elements of structural symmetry, and "gene duplication and fusion" is the evolutionary mechanism generally hypothesized to be responsible for their emergence from simple peptide motifs. Despite the central importance of the gene duplication and fusion hypothesis, experimental support for a plausible evolutionary pathway for a specific protein architecture has yet to be effectively demonstrated. To address this question, a unique "top-down symmetric deconstruction" strategy was utilized to successfully identify a simple peptide motif capable of recapitulating, via gene duplication and fusion processes, a symmetric protein architecture (the threefold symmetric β-trefoil fold). The folding properties of intermediary forms in this deconstruction agree precisely with a previously proposed "conserved architecture" model for symmetric protein evolution. Furthermore, a route through foldable sequence-space between the simple peptide motif and extant protein fold is demonstrated. These results provide compelling experimental support for a plausible evolutionary pathway of symmetric protein architecture via gene duplication and fusion processes.

PubMed: 21173271
DOI: 10.1073/pnas.1015032108

Experimental method

X-RAY DIFFRACTION (1.75 Å)