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Accepted (AM)Open Access (License Unspecified), Open
Journal article
Trapping of the Enoyl-Acyl Carrier Protein Reductase-Acyl Carrier Protein Interaction
Journal of the American Chemical Society, v 138(12), pp 3962-3965
30 Mar 2016
PMCID: PMC4988885
PMID: 26938266
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
An ideal target for metabolic engineering, fatty acid biosynthesis remains poorly understood on a molecular level. These carrier protein-dependent pathways require fundamental protein-protein interactions to guide reactivity and processivity, and their control has become one of the major hurdles in successfully adapting these biological machines. Our laboratory has developed methods to prepare acyl carrier proteins (ACPs) loaded with substrate mimetics and cross-linkers to visualize and trap interactions with partner enzymes, and we continue to expand the tools for studying these pathways. We now describe application of the slow-onset, tight-binding inhibitor triclosan to explore the interactions between the type II fatty acid ACP from Escherichia coli, AcpP, and its corresponding enoyl-ACP reductase, FabI. We show that the AcpP-triclosan complex demonstrates nM binding, inhibits in vitro activity, and can be used to isolate FabI in complex proteomes.
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Details
- Title
- Trapping of the Enoyl-Acyl Carrier Protein Reductase-Acyl Carrier Protein Interaction
- Creators
- Lorillee Tallorin - University of California, San DiegoKara Finzel - University of California, San DiegoQuynh G Nguyen - University of California, San DiegoJoris Beld - University of California, San DiegoJames J La Clair - University of California, San DiegoMichael D Burkart - University of California, San Diego
- Publication Details
- Journal of the American Chemical Society, v 138(12), pp 3962-3965
- Publisher
- American Chemical Society; Washington, DC
- Grant note
- R01 GM095970 / NIGMS NIH HHS F31 GM113470 / NIGMS NIH HHS F31GM113470 / NIGMS NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Microbiology and Immunology
- Web of Science ID
- WOS:000373518800007
- Scopus ID
- 2-s2.0-84964403890
- Other Identifier
- 991019168461004721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Chemistry, Multidisciplinary