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Curr Opin Chem Biol. 2016 Dec;35:89-96. doi: 10.1016/j.cbpa.2016.09.005. Epub 2016 Sep 25.

Structural insight into the necessary conformational changes of modular nonribosomal peptide synthetases.

Author information

1
Hauptman-Woodward Medical Research Institute, Buffalo, NY, USA; Department of Structural Biology, University at Buffalo, Buffalo, NY, USA. Electronic address: gulick@hwi.buffalo.edu.

Abstract

Nonribosomal peptide synthetases (NRPSs) catalyze the assembly line biosynthesis of peptide natural products that play important roles in microbial signaling and communication. These multidomain enzymes use an integrated carrier protein that delivers the growing peptide to the catalytic domains, requiring coordinated conformational changes that allow the proper sequence of synthetic steps. Recent structural studies of NRPSs have described important conformational states and illustrate the critical role of a small subdomain within the adenylation domains. This subdomain alternates between catalytic conformations and also serves as a linker domain, providing further conformational flexibility to enable the carrier to project from the core of NRPS. These studies are described along with remaining questions in the study of the structural dynamics of NRPSs.

PMID:
27676239
PMCID:
PMC5161630
DOI:
10.1016/j.cbpa.2016.09.005
[Indexed for MEDLINE]
Free PMC Article

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