ArticleNature communications2022
Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 29 citations in OpenAlex.
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- Activation of a Secondary-Messenger Receptor via Allosteric Modulation of a Dynamic Conformational Ensemble.Angewandte Chemie (International ed. in English) · 2025Article
- Bumps on the Road: The Way to Clean Relaxation Dispersion Magic-Angle Spinning NMR.Journal of the American Chemical Society · 2025Article
- OPTO: Automated Optimization for Solid-State NMR Spectroscopy.Journal of the American Chemical Society · 2025Article
- Dipolar Recoupling in Rotating Solids.Chemical reviews · 2024Review
- Protein deuterationChemical communications (Cambridge, England) · 2024Article
- Deuteration of proteins boosted by cell lysates: high-resolution amide and HMagnetic resonance (Gottingen, Germany) · 2024Article
- Allosteric communication between ligand binding domains modulates substrate inhibition in adenylate kinase.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Review
Corrections and comments
- Erratum issued
Authors and funding
10 authors at 3 institutions in 7 countries.
Funding
Abstract
Large oligomeric enzymes control a myriad of cellular processes, from protein synthesis and degradation to metabolism. The 0.5 MDa large TET2 aminopeptidase, a prototypical protease important for cellular homeostasis, degrades peptides within a ca. 60 Å wide tetrahedral chamber with four lateral openings. The mechanisms of substrate trafficking and processing remain debated. Here, we integrate magic-angle spinning (MAS) NMR, mutagenesis, co-evolution analysis and molecular dynamics simulations and reveal that a loop in the catalytic chamber is a key element for enzymatic function. The loop is able to stabilize ligands in the active site and may additionally have a direct role in activating the catalytic water molecule whereby a conserved histidine plays a key role. Our data provide a strong case for the functional importance of highly dynamic - and often overlooked - parts of an enzyme, and the potential of MAS NMR to investigate their dynamics at atomic resolution.
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Registered trials
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