期刊
CHEMISTRY & BIOLOGY
卷 17, 期 7, 页码 705-716出版社
CELL PRESS
DOI: 10.1016/j.chembiol.2010.05.017
关键词
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资金
- BBSRC [8/B18119]
- Universities UK
- Cambridge Australia Trust
- Cambridge Commonwealth Trust
- Corpus Christi College
- BBSRC [BB/E013228/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/E013228/1] Funding Source: researchfish
Numerous natural products of clinical value are bio-synthesized 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.
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