5c2n

The de novo evolutionary emergence of a symmetrical protein is shaped by folding constraints

spinqualitylabelsall models 5c2n, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5c2n is a 15 chain structure with sequence from Enterobacteria phage L1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.65Å Ligands: NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A140UHM9_9VIRU Publication Abstract from PubMed 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 beta-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., higher efficiency of folding, was the main parameter leading to improved functionality along the entire evolutionary trajectory. However, folding constraints changed along the trajectory: initially, conflicts between monomer folding and oligomer assembly dominated, whereas subsequently, upon tandem duplication, tradeoffs between monomer stability and foldability took precedence. De Novo Evolutionary Emergence of a Symmetrical Protein Is Shaped by Folding Constraints.,Smock RG, Yadid I, Dym O, Clarke J, Tawfik DS Cell. 2016 Jan 28;164(3):476-86. doi: 10.1016/j.cell.2015.12.024. Epub 2016 Jan, 21. PMID:26806127 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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