ArticleBiophysical journal2021
Structural basis for the hyperthermostability of an archaeal enzyme induced by succinimide formation.
Article in Biophysical journal, 2021. 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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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Insights into the role of internal catalysts in asparagine-to-succinimide conversion in a hyperthermophilic glutamine amidotransferase.The Journal of biological chemistry · 2026Article
- Aspartimide Modification in RiPP Natural Products.Biochemistry · 2026Review
- Cysimiditides: RiPPs with a Zn-Tetracysteine Motif and Aspartimidylation.Biochemistry · 2025Article
- GMP Synthetase: Allostery, Structure, and Function.Biomolecules · 2023Review
- Locking out water at 100°C.Biophysical journal · 2021Article
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Stability of proteins from hyperthermophiles (organisms existing under boiling water conditions) enabled by a reduction of conformational flexibility is realized through various mechanisms. A succinimide (SNN) arising from the post-translational cyclization of the side chains of aspartyl/asparaginyl residues with the backbone amide -NH of the succeeding residue would restrain the torsion angle Ψ and can serve as a new route for hyperthermostability. However, such a succinimide is typically prone to hydrolysis, transforming to either an aspartyl or β-isoaspartyl residue. Here, we present the crystal structure of Methanocaldococcus jannaschii glutamine amidotransferase and, using enhanced sampling molecular dynamics simulations, address the mechanism of its increased thermostability, up to 100°C, imparted by an unexpectedly stable succinimidyl residue at position 109. The stability of SNN109 to hydrolysis is seen to arise from its electrostatic shielding by the side-chain carboxylate group of its succeeding residue Asp110, as well as through n → π
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