ArticleProteins2014
The crystal structure of BlmI as a model for nonribosomal peptide synthetase peptidyl carrier proteins.
Article in Proteins, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 37 citations in OpenAlex.
- Nonribosomal peptide synthetases and their biotechnological potential in Penicillium rubens.Journal of industrial microbiology & biotechnology · 2021Review
- 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
- Elucidation of transient protein-protein interactions within carrier protein-dependent biosynthesis.Communications biology · 2021Article
- Biosynthesis of depsipeptides, or Depsi: The peptides with varied generations.Protein science : a publication of the Protein Society · 2020Review
- Type II non-ribosomal peptide synthetase proteins: structure, mechanism, and protein-protein interactions.Natural product reports · 2020Review
- Structural basis for chain release from the enacyloxin polyketide synthase.Nature chemistry · 2019Article
- Insights into Thiotemplated Pyrrole Biosynthesis Gained from the Crystal Structure of Flavin-Dependent Oxidase in Complex with Carrier Protein.Biochemistry · 2019Article
- New Structural Data Reveal the Motion of Carrier Proteins in Nonribosomal Peptide Synthesis.Angewandte Chemie (International ed. in English) · 2016Review
- Structure-based analysis of the molecular interactions between acyltransferase and acyl carrier protein in vicenistatin biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Synthetic cycle of the initiation module of a formylating nonribosomal peptide synthetase.Nature · 2016Article
- Loop dynamics of thymidine diphosphate-rhamnose 3'-O-methyltransferase (CalS11), an enzyme in calicheamicin biosynthesis.Structural dynamics (Melville, N.Y.) · 2016Article
- Structural Biology of Nonribosomal Peptide Synthetases.Methods in molecular biology (Clifton, N.J.) · 2016Article
- Crystal Structure of the Zorbamycin-Binding Protein ZbmA, the Primary Self-Resistance Element in Streptomyces flavoviridis ATCC21892.Biochemistry · 2015Article
- Solution Structure of a Nonribosomal Peptide Synthetase Carrier Protein Loaded with Its Substrate Reveals Transient, Well-Defined Contacts.Journal of the American Chemical Society · 2015Article
- Structure and Substrate Sequestration in the Pyoluteorin Type II Peptidyl Carrier Protein PltL.Journal of the American Chemical Society · 2015Article
- The structural biology of biosynthetic megaenzymes.Nature chemical biology · 2015Review
- Probing the phosphopantetheine arm conformations of acyl carrier proteins using vibrational spectroscopy.Journal of the American Chemical Society · 2014Article
- Structural and bioinformatic characterization of an Acinetobacter baumannii type II carrier protein.Acta crystallographica. Section D, Biological crystallography · 2014Article
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Authors and funding
9 authors at 4 institutions in 1 country.
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Abstract
Carrier proteins (CPs) play a critical role in the biosynthesis of various natural products, especially in nonribosomal peptide synthetase (NRPS) and polyketide synthase (PKS) enzymology, where the CPs are referred to as peptidyl-carrier proteins (PCPs) or acyl-carrier proteins (ACPs), respectively. CPs can either be a domain in large multifunctional polypeptides or standalone proteins, termed Type I and Type II, respectively. There have been many biochemical studies of the Type I PKS and NRPS CPs, and of Type II ACPs. However, recently a number of Type II PCPs have been found and biochemically characterized. In order to understand the possible interaction surfaces for combinatorial biosynthetic efforts we crystallized the first characterized and representative Type II PCP member, BlmI, from the bleomycin biosynthetic pathway from Streptomyces verticillus ATCC 15003. The structure is similar to CPs in general but most closely resembles PCPs. Comparisons with previously determined PCP structures in complex with catalytic domains reveals a common interaction surface. This surface is highly variable in charge and shape, which likely confers specificity for interactions. Previous nuclear magnetic resonance (NMR) analysis of a prototypical Type I PCP excised from the multimodular context revealed three conformational states. Comparison of the states with the structure of BlmI and other PCPs reveals that only one of the NMR states is found in other studies, suggesting the other two states may not be relevant. The state represented by the BlmI crystal structure can therefore serve as a model for both Type I and Type II PCPs.
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