3FG3: Crystal structure of Delta413-417:GS I805W LOX

Citation:
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.
PDB ID: 3FG3Download
MMDB ID: 155868
PDB Deposition Date: 2008/12/4
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
Similar Structures:
Biological Unit for 3FG3: monomeric; determined by author
Molecular Components in 3FG3
Label Count Molecule
Protein (1 molecule)
1
Allene Oxide Synthase-lipoxygenase Protein
Molecule annotation
Chemicals (24 molecules)
1
1
2
3
3
8
4
10
5
2
* Click molecule labels to explore molecular sequence information.

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