Article thumbnail
Location of Repository

Insights into protein-protein and enzyme-substrate interactions in modular polyketide synthases

By Lucky Tran, R. William Broadhurst, Manuela Tosin, Andrea Cavalli and Kira J. Weissman

Abstract

Numerous natural products of clinical value are biosynthesized by polyketide synthases (PKSs) and nonribosomal peptide synthetases (NRPSs), which are multienzymes comprising modules of catalytic domains. The key players in each module are carrier proteins, which serve as attachment points for the growing substrate chains. Thus, the details of carrier protein-based substrate delivery to each active site are central to understanding chain assembly in these systems. In the enterobactin NRPS, communication between a peptidyl carrier protein (PCP) and the adjacent thioesterase (TE) domain occurs through formation of a compact complex. Using NMR, we show that the corresponding interaction between a PKS acyl carrier protein (ACP) and its downstream TE is fundamentally different: chain transfer occurs in the absence of a protein-protein interface, with contact limited to the substrate acyl terminus

Topics: QD, QP
Publisher: Cell Press
Year: 2010
DOI identifier: 10.1016/j.chembiol.2010.05.017
OAI identifier: oai:wrap.warwick.ac.uk:40345
Download PDF:
Sorry, we are unable to provide the full text but you may find it at the following location(s):
  • http://dx.doi.org/10.1016/j.ch... (external link)
  • Suggested articles


    To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.