3FG1

Crystal structure of Delta413-417:GS LOX

Summary for 3FG1

• Entry DOI: 10.2210/pdb3fg1/pdb
• Related: 2FNQ 3FG3 3FG4
• Descriptor: Allene oxide synthase-lipoxygenase protein, FE (II) ION, CALCIUM ION, ... (7 entities in total)
• Functional Keywords: lipoxygenase, arichidonic metabolism, dioxygenase, fatty acid biosynthesis, heme, iron, lipid synthesis, lyase, membrane, metal-binding, multifunctional enzyme, oxidoreductase, oxylipin biosynthesis
• Biological source: Plexaura homomalla (black sea rod)
• Cellular location: Cytoplasm : O16025
• Total number of polymer chains: 4
• Total formula weight: 321892.05

Authors

Neau, D.B.,Newcomer, M.E. (deposition date: 2008-12-04, release date: 2009-08-18, Last modification date: 2023-09-06)

Primary citation

Neau, D.B.,Gilbert, N.C.,Bartlett, S.G.,Boeglin, W.,Brash, A.R.,Newcomer, M.E.
The 1.85 A structure of an 8R-lipoxygenase suggests a general model for lipoxygenase product specificity.
Biochemistry, 48:7906-7915, 2009

PubMed Abstract: Lipoxygenases (LOX) play pivotal roles in the biosynthesis of leukotrienes and other biologically active eicosanoids derived from arachidonic acid. A mechanistic understanding of substrate recognition, when lipoxygenases that recognize the same substrate generate different products, can be used to help guide the design of enzyme-specific inhibitors. We report here the 1.85 A resolution structure of an 8R-lipoxygenase from Plexaura homomalla, an enzyme with a sequence approximately 40% identical to that of human 5-LOX. The structure reveals a U-shaped channel, defined by invariant amino acids, that would allow substrate access to the catalytic iron. We demonstrate that mutations within the channel significantly impact enzyme activity and propose a novel model for substrate binding potentially applicable to other members of this enzyme family.

PubMed: 19594169
DOI: 10.1021/bi900084m

Experimental method

X-RAY DIFFRACTION (1.85 Å)