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Acyl Carrier Protein Cyanylation Delivers a Ketoacyl Synthase–Carrier Protein Cross-Link
Journal article   Open access   Peer reviewed

Acyl Carrier Protein Cyanylation Delivers a Ketoacyl Synthase–Carrier Protein Cross-Link

Grace A. R Thiele, Connie P Friedman, Kathleen J. S Tsai, Joris Beld, Casey H Londergan and Louise K Charkoudian
Biochemistry (Easton), v 56(20), pp 2533-2536
23 May 2017
DOI: https://doi.org/10.1021/acs.biochem.7b00219
PMID: 28448715
Featured in Collection :   UN Sustainable Development Goals @ Drexel
url
https://europepmc.org/articles/pmc5590888View
Accepted (AM) Open Open Access (License Unspecified)

Abstract

Acyl carrier proteins (ACPs) are central hubs in polyketide and fatty acid biosynthetic pathways, but the fast motions of the ACP’s phosphopantetheine (Ppant) arm make its conformational dynamics difficult to capture using traditional spectroscopic approaches. Here we report that converting the terminal thiol of Escherichia coli ACP’s Ppant arm into a thiocyanate activates this site to form a selective cross-link with the active site cysteine of its partner ketoacyl synthase (FabF). The reaction releases a cyanide anion, which can be detected by infrared spectroscopy. This represents a practical and generalizable method for obtaining and visualizing ACP–protein complexes relevant to biocatalysis and will be valuable in future structural and engineering studies.

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11 citations in Web of Science
11 citations in Scopus

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Collaboration types
Domestic collaboration
Web of Science research areas
Biochemistry & Molecular Biology
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