Molecular evolution has focused on the divergence of molecular functions, yet we know little about how structurally distinct protein folds emerge de novo. We characterized the evolutionary trajectories and selection forces underlying emergence of β-propeller proteins, a globular and symmetric fold group with diverse functions. The identification of short propeller-like motifs (<50 amino acids) in natural genomes indicated that they expanded via tandem duplications to form extant propellers. We phylogenetically reconstructed 47-residue ancestral motifs that form five-bladed lectin propellers via oligomeric assembly. We demonstrate a functional trajectory of tandem duplications of these motifs leading to monomeric lectins. Foldability, i.e., ...
Going down the folding funnel, proteins may sample a wide variety of conformations, some being outri...
<div><p>Nature has shaped the make up of proteins since their appearance, 3.8 billion years ago. How...
e o evolved via duplication and recombination of smaller functional elements. *Corresponding author ...
International audienceLectins with a β-propeller fold bind glycans on the cell surface through multi...
International audienceLectins with a β-propeller fold bind glycans on the cell surface through multi...
Lectins with a β-propeller fold bind glycans on the cell surface through multivalent binding sites a...
International audienceLectins with a β-propeller fold bind glycans on the cell surface through multi...
β-propeller proteins are common in nature, where they are observed to adopt 4- to 10-fold internal r...
Since the time of the Last Universal Common Ancestor (LUCA), proteins have been the fundamental cata...
β-Propellers are toroidal folds, in which repeated, four-stranded β-meanders are arranged in a circu...
Since the time of the Last Universal Common Ancestor (LUCA), proteins have been the fundamental cata...
Even a relatively short polypeptide of 75 amino acids has more unique sequence possibilities than th...
SummaryModels of symmetric protein evolution typically invoke gene duplication and fusion events, in...
SummaryThe high frequency of internal structural symmetry in common protein folds is presumed to ref...
Going down the folding funnel, proteins may sample a wide variety of conformations, some being outri...
Going down the folding funnel, proteins may sample a wide variety of conformations, some being outri...
<div><p>Nature has shaped the make up of proteins since their appearance, 3.8 billion years ago. How...
e o evolved via duplication and recombination of smaller functional elements. *Corresponding author ...
International audienceLectins with a β-propeller fold bind glycans on the cell surface through multi...
International audienceLectins with a β-propeller fold bind glycans on the cell surface through multi...
Lectins with a β-propeller fold bind glycans on the cell surface through multivalent binding sites a...
International audienceLectins with a β-propeller fold bind glycans on the cell surface through multi...
β-propeller proteins are common in nature, where they are observed to adopt 4- to 10-fold internal r...
Since the time of the Last Universal Common Ancestor (LUCA), proteins have been the fundamental cata...
β-Propellers are toroidal folds, in which repeated, four-stranded β-meanders are arranged in a circu...
Since the time of the Last Universal Common Ancestor (LUCA), proteins have been the fundamental cata...
Even a relatively short polypeptide of 75 amino acids has more unique sequence possibilities than th...
SummaryModels of symmetric protein evolution typically invoke gene duplication and fusion events, in...
SummaryThe high frequency of internal structural symmetry in common protein folds is presumed to ref...
Going down the folding funnel, proteins may sample a wide variety of conformations, some being outri...
Going down the folding funnel, proteins may sample a wide variety of conformations, some being outri...
<div><p>Nature has shaped the make up of proteins since their appearance, 3.8 billion years ago. How...
e o evolved via duplication and recombination of smaller functional elements. *Corresponding author ...