ArticleBiochemistry2020
An Unusually Rapid Protein Backbone Modification Stabilizes the Essential Bacterial Enzyme MurA.
Article in Biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 14 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
- Repurposing Azeliragon as a novel antibacterial agent against methicillin-resistant Staphylococcus aureus via combined membrane phospholipids and cell wall targeting.Communications biology · 2026Article
- Advanced NMR Characterization and Sensitive Detection of Isoaspartate in Proteins.Analytical chemistry · 2026Article
- Aspartimide Modification in RiPP Natural Products.Biochemistry · 2026Review
- Effects of legume-based rotation on subsequent sorghum rhizosphere microbial communities and their drought tolerance-related genes.Environmental microbiome · 2026Article
- Structural basis for sequence context-independent single-stranded DNA cytosine deamination by the bacterial toxin SsdA.Nature communications · 2025Article
- Semisynthesis of Isomerized Histone H4 Reveals Robustness and Vulnerability of Chromatin toward Molecular Aging.Journal of the American Chemical Society · 2025Article
- Stability of Protein Pharmaceuticals: Recent Advances.Pharmaceutical research · 2024Review
- Conformational Control of Fast Asparagine Deamidation in a Norovirus Capsid Protein.Biochemistry · 2023Article
- In vivo, in vitro and in silico: an open space for the development of microbe-based applications of synthetic biology.Microbial biotechnology · 2022Article
- Structural basis for the hyperthermostability of an archaeal enzyme induced by succinimide formation.Biophysical journal · 2021Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Proteins are subject to spontaneous rearrangements of their backbones. Most prominently, asparagine and aspartate residues isomerize to their β-linked isomer, isoaspartate (isoAsp), on time scales ranging from days to centuries. Such modifications are typically considered "molecular wear-and-tear", destroying protein function. However, the observation that some proteins, including the essential bacterial enzyme MurA, harbor stoichiometric amounts of isoAsp suggests that this modification can confer advantageous properties. Here, we demonstrate that nature exploits an isoAsp residue within a hairpin to stabilize MurA. We found that isoAsp formation in MurA is unusually rapid and critically dependent on folding status. Moreover, perturbation of the isoAsp-containing hairpin via site-directed mutagenesis causes aggregation of MurA variants. Structural mass spectrometry revealed that this effect is caused by local protein unfolding in MurA mutants. Our findings demonstrate that MurA evolved to "mature" via a spontaneous post-translational incorporation of a β-amino acid, which raises the possibility that isoAsp-containing hairpins may serve as a structural motif of biological importance.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.