ArticleProtein science : a publication of the Protein Society2020
Influence of circular permutations on the structure and stability of a six-fold circular symmetric designer protein.
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 5 papers.
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5 citing papers in PubMed.
- Circular permutation at azurin's active site slows down its folding.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023Article
- Review
- Stability profile of vimentin rod domain.Protein science : a publication of the Protein Society · 2022Article
- Structure and stability of the designer protein WRAP-T and its permutants.Scientific reports · 2021Article
- Influence of circular permutations on the structure and stability of a six-fold circular symmetric designer protein.Protein science : a publication of the Protein Society · 2020Article
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6 authors.
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Abstract
The β-propeller fold is adopted by a sequentially diverse family of repeat proteins with apparent rotational symmetry. While the structure is mostly stabilized by hydrophobic interactions, an additional stabilization is provided by hydrogen bonds between the N-and C-termini, which are almost invariably part of the same β-sheet. This feature is often referred to as the "Velcro" closure. The positioning of the termini within a blade is variable and depends on the protein family. In order to investigate the influence of this location on protein structure, folding and stability, we created different circular permutants, and a circularized version, of the designer propeller protein named Pizza. This protein is perfectly symmetrical, possessing six identical repeats. While all mutants adopt the same structure, the proteins lacking the "Velcro" closure were found to be significantly less resistant to thermal and chemical denaturation. This could explain why such proteins are rarely observed in nature. Interestingly the most common "Velcro" configuration for this protein family was not the most stable among the Pizza variants tested. The circularized version shows dramatically improved stability, which could have implications for future applications.
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