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A covalent linker allows for membrane targeting of an oxylipin biosynthetic complex
Authors
Sue G. Bartlett
Tee Bordelon
+7 more
Alan R. Brash
Adam Dassey
Nathaniel C. Gilbert
Marcia E. Newcomer
Marc Niebuhr
Oswin Ridderbusch
Hiro Tsuruta
Publication date
7 October 2008
Publisher
LSU Digital Commons
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Abstract
A naturally occurring bifunctional protein from Plexaura homomalla links sequential catalytic activities in an oxylipin biosynthetic pathway. The C-terminal lipoxygenase (LOX) portion of the molecule catalyzes the transformation of arachidonic acid (AA) to the corresponding 8R-hydroperoxide, and the N-terminal allene oxide synthase (AOS) domain promotes the conversion of the hydroperoxide intermediate to the product allene oxide (AO). Small-angle X-ray scattering data indicate that in the absence of a covalent linkage the two catalytic domains that transform AA to AO associate to form a complex that recapitulates the structure of the bifunctional protein. The SAXS data also support a model for LOX and AOS domain orientation in the fusion protein inferred from a low-resolution crystal structure. However, results of membrane binding experiments indicate that covalent linkage of the domains is required for Ca2+-dependent membrane targeting of the sequential activities, despite the noncovalent domain association. Furthermore, membrane targeting is accompanied by a conformational change as monitored by specific proteolysis of the linker that joins the AOS and LOX domains. Our data are consistent with a model in which Ca2+-dependent membrane binding relieves the noncovalent interactions between the AOS and LOX domains and suggests that the C2-like domain of LOX mediates both protein-protein and protein-membrane interactions. © 2008 American Chemical Society
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Louisiana State University
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Last time updated on 26/10/2023
Louisiana State University
See this paper in CORE
Go to the repository landing page
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oai:repository.lsu.edu:chemist...
Last time updated on 26/10/2023