Journal
CHEMISTRY & BIOLOGY
Volume 18, Issue 11, Pages 1482-1488Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2011.09.018
Keywords
-
Categories
Funding
- NIH [GM086570]
- NSF [CAREER-0645653]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1032769] Funding Source: National Science Foundation
Ask authors/readers for more resources
Phosphopantetheine-modified carrier domains play a central role in the template-directed, biosynthesis of several classes of primary and secondary metabolites. Fatty acids, polyketides, and nonribosomal peptides are constructed on multidomain enzyme assemblies using phosphopantetheinyl thioester-linked carrier domains to traffic and activate building blocks. The carrier domain is a dynamic component of the process, shuttling pathway intermediates to sequential enzyme active sites. Here, we report an approach to structurally fix carrier domain/enzyme constructs suitable for X-ray crystallographic analysis. The structure of a two-domain construct of Escherichia coli EntF was determined with a conjugated phosphopantetheinyl-based inhibitor. The didomain structure is locked in an active orientation relevant to the chemistry of nonribosomal peptide biosynthesis. This structure provides details into the interaction of phosphopantetheine arm with the carrier domain and the active site of the thioesterase domain.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available