ArticleBiochemistry2017
Manipulating Protein-Protein Interactions in Nonribosomal Peptide Synthetase Type II Peptidyl Carrier Proteins.
Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Interface Engineering of Carrier-Protein-Dependent Metabolic Pathways.ACS chemical biology · 2023Article
- The Assembly-Line Enzymology of Nonribosomal Peptide Biosynthesis.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Essential Role of Loop Dynamics in Type II NRPS Biomolecular Recognition.ACS chemical biology · 2022Article
- Protein-protein interface analysis of the non-ribosomal peptide synthetase peptidyl carrier protein and enzymatic domains.Synthetic and systems biotechnology · 2022Review
- Elucidation of transient protein-protein interactions within carrier protein-dependent biosynthesis.Communications biology · 2021Article
- Dynamic visualization of type II peptidyl carrier protein recognition in pyoluteorin biosynthesis.RSC chemical biology · 2020Article
- Type II non-ribosomal peptide synthetase proteins: structure, mechanism, and protein-protein interactions.Natural product reports · 2020Review
- 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
- Alanine Scanning of YbdZ, an MbtH-like Protein, Reveals Essential Residues for Functional Interactions with Its Nonribosomal Peptide Synthetase Partner EntF.Biochemistry · 2018Article
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Authors and funding
7 authors.
Funding
Abstract
In an effort to elucidate and engineer interactions in type II nonribosomal peptide synthetases, we analyzed biomolecular recognition between the essential peptidyl carrier proteins and adenylation domains using nuclear magnetic resonance (NMR) spectroscopy, molecular dynamics, and mutational studies. Three peptidyl carrier proteins, PigG, PltL, and RedO, in addition to their cognate adenylation domains, PigI, PltF, and RedM, were investigated for their cross-species activity. Of the three peptidyl carrier proteins, only PigG showed substantial cross-pathway activity. Characterization of the novel NMR solution structure of holo-PigG and molecular dynamics simulations of holo-PltL and holo-PigG revealed differences in structures and dynamics of these carrier proteins. NMR titration experiments revealed perturbations of the chemical shifts of the loop 1 residues of these peptidyl carrier proteins upon their interaction with the adenylation domain. These experiments revealed a key region for the protein-protein interaction. Mutational studies supported the role of loop 1 in molecular recognition, as mutations to this region of the peptidyl carrier proteins significantly modulated their activities.
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