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. Author manuscript; available in PMC: 2016 Jan 2.
Published in final edited form as: Mol Biosyst. 2014 Oct 31;11(1):38–59. doi: 10.1039/c4mb00443d

Figure 2.

Figure 2

Cartoon of cargo sequestration and chain-flipping mechanism by acyl carrier proteins. a) the acyl carrier protein (ACP, grey protein cartoon structure) is post-translationally modified with a 4′-phosphopantetheine arm, bearing a terminal thiol. b) when a fatty acid intermediate (yellow rectangle) is loaded onto the 4′-phosphopantetheine moiety, it is protected from the environment by sequestration in the inner core of the ACP. c) a partner protein (orange) binds to the ACP. d) the protein-protein binding event induces a conformational change in the carrier protein, allowing the cargo to flip out of the inner core into the active site of the partner enzyme (the “chain-flipping mechanism”). e) chemical transformation of the fatty acid intermediate (yellow > red) occurs in the active site of the partner enzyme. f) after the reaction is complete the partner enzyme leaves, and another partner protein (blue) can bind to the ACP.

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