3dy5

Allene oxide synthase 8R-lipoxygenase from Plexaura homomalla

spinqualitylabelsall models 3dy5, resolution 3.51Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3dy5 is a 2 chain structure with sequence from Black sea rod. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FE2, HEM Related: 1u5u, 2fnq Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [AOSL_PLEHO] Bifunctional enzyme which is responsible for allene oxide biosynthesis via a two-step reaction which involves conversion of arachidonic acid to a 8R-hydroperoxide intermediate followed by conversion of the hydroperoxide to allene oxide. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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 8 R-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 Ca (2+)-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 Ca (2+)-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. A covalent linker allows for membrane targeting of an oxylipin biosynthetic complex.,Gilbert NC, Niebuhr M, Tsuruta H, Bordelon T, Ridderbusch O, Dassey A, Brash AR, Bartlett SG, Newcomer ME Biochemistry. 2008 Oct 7;47(40):10665-76. Epub 2008 Sep 12. PMID:18785758 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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