ArticleNature chemical biology2015
Secondary structure reshuffling modulates glycosyltransferase function at the membrane.
Article in Nature chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 52 citations in OpenAlex.
- Comparative study of two xanthan gum glycosyltransferases combining AI structure predictions and molecular modeling.bioRxiv : the preprint server for biology · 2026Article
- Functional and mechanistic characterization of the phosphatidyl-Frontiers in cellular and infection microbiology · 2026Article
- Mapping the energy landscape of a fold-switching protein MAD2.Protein science : a publication of the Protein Society · 2025Article
- Bioinformatic analysis of rare endothelial protein C receptor missense variants associated with coagulation and thrombophilia risk.Scientific reports · 2025Article
- Structure and membrane interactions of Arabidopsis thaliana DGD2, a glycosyltransferase in the chloroplast membrane.The Journal of biological chemistry · 2025Article
- Cryo-EM analysis ofScience advances · 2024Article
- Substrate binding and catalytic mechanism of the Se-glycosyltransferase SenB in the biosynthesis of selenoneine.Nature communications · 2024Article
- Fluid protein fold space and its implications.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Self-recycling and partially conservative replication of mycobacterial methylmannose polysaccharides.Communications biology · 2023Article
- Many dissimilar NusG protein domains switch between α-helix and β-sheet folds.Nature communications · 2022Article
- Article
- AlphaFold2 fails to predict protein fold switching.Protein science : a publication of the Protein Society · 2022Article
- Metamorphic proteins under a computational microscope: Lessons from a fold-switching RfaH protein.Computational and structural biotechnology journal · 2022Review
- Molecular ruler mechanism and interfacial catalysis of the integral membrane acyltransferase PatA.Science advances · 2021Article
- Secondary-structure switch regulates the substrate binding of a YopJ family acetyltransferase.Nature communications · 2021Article
- A sequence-based method for predicting extant fold switchers that undergo α-helix ↔ β-strand transitions.Biopolymers · 2021Article
- Predictable fold switching by the SARS-CoV-2 protein ORF9b.Protein science : a publication of the Protein Society · 2021Article
- ProteinMolecules (Basel, Switzerland) · 2021Article
- The Phosphatidyl-Journal of bacteriology · 2021Article
- Functional and Regulatory Roles of Fold-Switching Proteins.Structure (London, England : 1993) · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Secondary structure refolding is a key event in biology as it modulates the conformation of many proteins in the cell, generating functional or aberrant states. The crystal structures of mannosyltransferase PimA reveal an exceptional flexibility of the protein along the catalytic cycle, including β-strand-to-α-helix and α-helix-to-β-strand transitions. These structural changes modulate catalysis and are promoted by interactions of the protein with anionic phospholipids in the membrane.
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Registered trials
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.