PDBsum entry 3o4c

De novo protein

PDB id: 3o4c

Contents

Protein chain

124 a.a. *

Ligands

TRS

SO4 ×2

Metals

_CL ×2

Waters ×78

* Residue conservation analysis

PDB id:

3o4c

Name:

De novo protein

Title:

Crystal structure of symfoil-4v: de novo designed beta-trefoil architecture with symmetric primary structure

Structure:

De novo designed beta-trefoil architecture with symmetric primary structure. Chain: a. Engineered: yes

Source:

Synthetic construct. Artificial gene. Organism_taxid: 32630. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.75Å R-factor: 0.196 R-free: 0.224

Authors:

J.Lee,M.Blaber

Key ref:

J.Lee and M.Blaber (2011). Experimental support for the evolution of symmetric protein architecture from a simple peptide motif. Proc Natl Acad Sci U S A, 108, 126-130. PubMed id: 21173271

Date:

26-Jul-10 Release date: 22-Dec-10

Protein chain

No UniProt id for this chain

Struc: 124 a.a.

Proc Natl Acad Sci U S A 108:126-130 (2011)

PubMed id: 21173271

Experimental support for the evolution of symmetric protein architecture from a simple peptide motif.

J.Lee, M.Blaber.

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.