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Cited by 185

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Structural insights into nonribosomal peptide enzymatic assembly lines

Open access
Koglin, Alexander, Walsh, Christopher T.·2009·Natural Product Reports

Abstract

Nonribosomal peptides have a variety of medicinal activities including activity as antibiotics, antitumor drugs, immunosuppressives, and toxins. Their biosynthesis on multimodular assembly lines as a series of covalently tethered thioesters, in turn covalently attached on pantetheinyl arms on carrier protein way stations, reflects similar chemical logic and protein machinery to fatty acid and polyketide biosynthesis. While structural information on excised or isolated catalytic adenylation (A), condensation (C), peptidyl carrier protein (PCP) and thioesterase (TE) domains had been gathered over the past decade, little was known about how the NRPS catalytic and carrier domains interact with each other both within and across elongation or termination modules. This Highlight reviews recent breakthrough achievements in both X-ray and NMR spectroscopic studies that illuminate the architecture of NRPS PCP domains, PCP-containing didomain-fragments and of a full termination module (C-A-PCP-TE).

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Metadata

Authors
Koglin, A., & Walsh, C. T.
Venue
Natural Product Reports
Published
2009
Volume
26
Issue
8
Pages
987
ISSN
  • 0265-0568 (ISSN-L)
  • 1460-4752
OpenAlex
W2061278426
Cited by
185
References
2
FWCI
13.45
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Structural insights into nonribosomal peptide enzymatic assembly lines. https://app.cochat.ai/papers/10.1039/b904543k
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Koglin, A., & Walsh, C. T. (2009). Structural insights into nonribosomal peptide enzymatic assembly lines. Natural Product Reports. https://doi.org/10.1039/b904543k

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.