ArticleFEBS open bio2014
Ancestral mutations as a tool for solubilizing proteins: The case of a hydrophobic phosphate-binding protein.
Article in FEBS open bio, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Ancestral sequence reconstruction as a tool for structural analysis of modular polyketide synthases.Nature communications · 2025Article
- A Reconstructed Common Ancestor of the Fatty Acid Photo-decarboxylase Clade Shows Photo-decarboxylation Activity and Increased Thermostability.Chembiochem : a European journal of chemical biology · 2021Article
- Engineering of Ancestors as a Tool to Elucidate Structure, Mechanism, and Specificity of Extant Terpene Cyclase.Journal of the American Chemical Society · 2021Article
- Immunological Study of Reconstructed Common Ancestral Sequence of Adenovirus Hexon Protein.Frontiers in microbiology · 2021Article
- Highly thermostable carboxylic acid reductases generated by ancestral sequence reconstruction.Communications biology · 2019Article
- Rational engineering of a native hyperthermostable lactonase into a broad spectrum phosphotriesterase.Scientific reports · 2017Article
- Ancestral protein resurrection and engineering opportunities of the mamba aminergic toxins.Scientific reports · 2017Article
- AAV ancestral reconstruction library enables selection of broadly infectious viral variants.Gene therapy · 2015Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Stable and soluble proteins are ideal candidates for functional and structural studies. Unfortunately, some proteins or enzymes can be difficult to isolate, being sometimes poorly expressed in heterologous systems, insoluble and/or unstable. Numerous methods have been developed to address these issues, from the screening of various expression systems to the modification of the target protein itself. Here we use a hydrophobic, aggregation-prone, phosphate-binding protein (HPBP) as a case study. We describe a simple and fast method that selectively uses ancestral mutations to generate a soluble, stable and functional variant of the target protein, here named sHPBP. This variant is highly expressed in Escherichia coli, is easily purified and its structure was solved at much higher resolution than its wild-type progenitor (1.3 versus 1.9 Å, respectively).
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Registered trials
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