Tran, Lucky, Broadhurst, R. William, Tosin, Manuela, Cavalli, Andrea and Weissman, Kira J.. (2010) Insights into protein-protein and enzyme-substrate interactions in modular polyketide synthases. Chemistry & Biology, Vol.17 (No.7). pp. 705-716. ISSN 1074-5521

Full text not available from this repository.

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.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry Q Science > QP Physiology
Divisions:	Faculty of Science > Chemistry
Library of Congress Subject Headings (LCSH):	Protein-protein interactions, Polyketides -- Synthesis, Carrier proteins, Enzymes
Journal or Publication Title:	Chemistry & Biology
Publisher:	Cell Press
ISSN:	1074-5521
Official Date:	2010
Volume:	Vol.17
Number:	No.7
Page Range:	pp. 705-716
Identification Number:	10.1016/j.chembiol.2010.05.017
Status:	Peer Reviewed
Publication Status:	Published
Funder:	Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC)
Grant number:	8/B18119 (BBSRC)
URI:	http://wrap.warwick.ac.uk/id/eprint/40345

Request changes or add full text files to a record

Actions (login required)

View Item