ArticleJournal of the American Chemical Society2015
Solution Structure of a Nonribosomal Peptide Synthetase Carrier Protein Loaded with Its Substrate Reveals Transient, Well-Defined Contacts.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 45 citations in OpenAlex.
- The specificity of intermodular recognition in a prototypical nonribosomal peptide synthetase depends on an adaptor domain.Science advances · 2024Article
- Probing Substrate-Loaded Carrier Proteins by Nuclear Magnetic Resonance.Methods in molecular biology (Clifton, N.J.) · 2023Article
- NMR as a readout to monitor and restore the integrity of complex chemoenzymatic reactions.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2022Article
- Global protein dynamics as communication sensors in peptide synthetase domains.Science advances · 2022Article
- Nonribosomal peptide synthetases and their biotechnological potential in Penicillium rubens.Journal of industrial microbiology & biotechnology · 2021Review
- Finding Druggable Sites in Proteins Using TACTICS.Journal of chemical information and modeling · 2021Article
- Cooperation between a T Domain and a Minimal C-Terminal Docking Domain to Enable Specific Assembly in a Multiprotein NRPS.Angewandte Chemie (International ed. in English) · 2021Article
- Using delayed decoupling to attenuate residual signals in editing filters.Magnetic resonance (Gottingen, Germany) · 2021Article
- Article
- Context-dependent activity of A domains in the tyrocidine synthetase.Scientific reports · 2019Article
- Insights into Thiotemplated Pyrrole Biosynthesis Gained from the Crystal Structure of Flavin-Dependent Oxidase in Complex with Carrier Protein.Biochemistry · 2019Article
- Trapping interactions between catalytic domains and carrier proteins of modular biosynthetic enzymes with chemical probes.Natural product reports · 2018Review
- Manipulating Protein-Protein Interactions in Nonribosomal Peptide Synthetase Type II Peptidyl Carrier Proteins.Biochemistry · 2017Article
- FRET monitoring of a nonribosomal peptide synthetase.Nature chemical biology · 2017Article
- Molecular impact of covalent modifications on nonribosomal peptide synthetase carrier protein communication.The Journal of biological chemistry · 2017Article
- Molecular Cross-Talk between Nonribosomal Peptide Synthetase Carrier Proteins and Unstructured Linker Regions.Chembiochem : a European journal of chemical biology · 2017Article
- Covariance nuclear magnetic resonance methods for obtaining protein assignments and novel correlations.Concepts in magnetic resonance. Part A, Bridging education and research · 2017Article
- Structural insight into the necessary conformational changes of modular nonribosomal peptide synthetases.Current opinion in chemical biology · 2016Review
- New Structural Data Reveal the Motion of Carrier Proteins in Nonribosomal Peptide Synthesis.Angewandte Chemie (International ed. in English) · 2016Review
- Sticky swinging arm dynamics: studies of an acyl carrier protein domain from the mycolactone polyketide synthase.The Biochemical journal · 2016Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Nonribosomal peptide synthetases (NRPSs) are microbial enzymes that produce a wealth of important natural products by condensing substrates in an assembly line manner. The proper sequence of substrates is obtained by tethering them to phosphopantetheinyl arms of holo carrier proteins (CPs) via a thioester bond. CPs in holo and substrate-loaded forms visit NRPS catalytic domains in a series of transient interactions. A lack of structural information on substrate-loaded carrier proteins has hindered our understanding of NRPS synthesis. Here, we present the first structure of an NRPS aryl carrier protein loaded with its substrate via a native thioester bond, together with the structure of its holo form. We also present the first quantification of NRPS CP backbone dynamics. Our results indicate that prosthetic moieties in both holo and loaded forms are in contact with the protein core, but they also sample states in which they are disordered and extend in solution. We observe that substrate loading induces a large conformational change in the phosphopantetheinyl arm, thereby modulating surfaces accessible for binding to other domains. Our results are discussed in the context of NRPS domain interactions.
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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.