ArticleProtein science : a publication of the Protein Society2020
Conserved buried water molecules enable the β-trefoil architecture.
Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed.
- Residue-Specific Signatures of Structural Water Identified by Dissolution Dynamic Nuclear Polarization with UV-Generated Radicals.Angewandte Chemie (International ed. in English) · 2026Article
- Functionalization of a symmetric protein scaffold: Redundant folding nuclei and alternative oligomeric folding pathways.Protein science : a publication of the Protein Society · 2022Article
- Evidence for the emergence of β-trefoils by 'Peptide Budding' from an IgG-like β-sandwich.PLoS computational biology · 2022Article
- Variable and Conserved Regions of Secondary Structure in the β-Trefoil Fold: Structure Versus Function.Frontiers in molecular biosciences · 2022Article
- The ubiquitous buried water in the beta-trefoil architecture contributes to the folding nucleus and ~20% of the folding enthalpy.Protein science : a publication of the Protein Society · 2021Article
- Cooperative hydrophobic core interactions in the β-trefoil architecture.Protein science : a publication of the Protein Society · 2021Article
- Conserved buried water molecules enable the β-trefoil architecture.Protein science : a publication of the Protein Society · 2020Article
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Abstract
Available high-resolution crystal structures for the family of β-trefoil proteins in the structural databank were queried for buried waters. Such waters were classified as either: (a) unique to a particular domain, family, or superfamily or (b) conserved among all β-trefoil folds. Three buried waters conserved among all β-trefoil folds were identified. These waters are related by the threefold rotational pseudosymmetry characteristic of this protein architecture (representing three instances of an identical structural environment within each repeating trefoil-fold motif). The structural properties of this buried water are remarkable and include: residing in a cavity space no larger than a single water molecule, exhibiting a positional uncertainty (i.e., normalized B-factor) substantially lower than the average Cα atom, providing essentially ideal H-bonding geometry with three solvent-inaccessible main chain groups, simultaneously serving as a bridging H-bond for three different β-strands at a point of secondary structure divergence, and orienting conserved hydrophobic side chains to form a nascent core-packing group. Other published work supports an interpretation that these interactions are key to the formation of an efficient folding nucleus and folded thermostability. The fundamental threefold symmetric structural element of the β-trefoil fold is therefore, surprisingly, a buried water molecule.
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