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Crystal Structure of the Termination Module of a Nonribosomal Peptide Synthetase
Abstract
Nonribosomal peptide synthetases (NRPSs) are modular multidomain enzymes that act as an assembly line to catalyze the biosynthesis of complex natural products. The crystal structure of the 144-kilodalton Bacillus subtilis termination module SrfA-C was solved at 2.6 angstrom resolution. The adenylation and condensation domains of SrfA-C associate closely to form a catalytic platform, with their active sites on the same side of the platform. The peptidyl carrier protein domain is flexibly tethered to this platform and thus can move with its substrate-loaded 4′-phosphopantetheine arm between the active site of the adenylation domain and the donor side of the condensation domain. The SrfA-C crystal structure has implications for the rational redesign of NRPSs as a means of producing novel bioactive peptides.
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Cited by
Surfactin and Other Lipopeptides from Bacillus spp.
Jacques, P. (2011) · Microbiology Monographs · doi:10.1007/978-3-642-14490-5_3 · Cited by 214
The Landscape of Recombination Events That Create Nonribosomal Peptide Diversity
Baunach, M., Chowdhury, S., Stallforth, P., & Dittmann, E. (2021) · Molecular Biology and Evolution · doi:10.1093/molbev/msab015 · Cited by 72
Dey, R., Valle, D. O., Chakraborty, A., Mayer, K. A., Uppala, J. K., Chakraborty, A., Mirza, S., Skwor, T., Forst, S., & Dey, M. (2025) · Frontiers in Microbiology · doi:10.3389/fmicb.2025.1560663 · Cited by 1
Metadata
- Authors
- Tanovic, A., Samel, S. A., Essen, L.-O., & Marahiel, M. A.
- Venue
- Science
- Published
- 2008-08
- Volume
- 321
- Issue
- 5889
- Pages
- 659-663
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2059504647
- Cited by
- 337
- References
- 0
- FWCI
- 12.21
- Type
- journal article
- Language
- en
- Open access
- closed
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