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Issue 8, 2009

Structural insights into nonribosomal peptide enzymatic assembly lines

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Abstract

Covering: up to the end of 2008

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).

Graphical abstract: Structural insights into nonribosomal peptide enzymatic assembly lines

Article information


Submitted
05 Mar 2009
First published
22 May 2009

Nat. Prod. Rep., 2009,26, 987-1000
Article type
Highlight

Structural insights into nonribosomal peptide enzymatic assembly lines

A. Koglin and C. T. Walsh, Nat. Prod. Rep., 2009, 26, 987 DOI: 10.1039/B904543K

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