Structures of single-layer β-sheet proteins evolved from β-hairpin repeats
| Autor: | Xu, Qingping, Biancalana, Matthew, Grant, Joanna C, Chiu, Hsiu-Ju, Jaroszewski, Lukasz, Knuth, Mark W, Lesley, Scott A, Godzik, Adam, Elsliger, Marc-André, Deacon, Ashley M, Wilson, Ian A |
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| Rok vydání: | 2019 |
| Předmět: |
Protein Folding
Protein Conformation β-hairpin repeats 1.1 Normal biological development and functioning Biophysics secreted proteins Bacterial Proteins Models Underpinning research single-layer beta-sheet proteins Other Information and Computing Sciences human gut microbiome Crystallography Bacteria Molecular Hydrogen Bonding beta-hairpin repeats Computation Theory and Mathematics structural genomics Gastrointestinal Microbiome X-Ray Tyrosine beta-Strand Biochemistry and Cell Biology Hydrophobic and Hydrophilic Interactions single-layer β-sheet proteins |
| Zdroj: | Protein science : a publication of the Protein Society, vol 28, iss 9 |
| Popis: | Free-standing single-layer β-sheets are extremely rare in naturally occurring proteins, even though β-sheet motifs are ubiquitous. Here we report the crystal structures of three homologous, single-layer, anti-parallel β-sheet proteins, comprised of three or four twisted β-hairpin repeats. The structures reveal that, in addition to the hydrogen bond network characteristic of β-sheets, additional hydrophobic interactions mediated by small clusters of residues adjacent to the turns likely play a significant role in the structural stability and compensate for the lack of a compact hydrophobic core. These structures enabled identification of a family of secreted proteins that are broadly distributed in bacteria from the human gut microbiome and are putatively involved in the metabolism of complex carbohydrates. A conserved surface patch, rich in solvent-exposed tyrosine residues, was identified on the concave surface of the β-sheet. These new modular single-layer β-sheet proteins may serve as a new model system for studying folding and design of β-rich proteins. |
| Databáze: | OpenAIRE |
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