1LOX

RABBIT RETICULOCYTE 15-LIPOXYGENASE

Summary for 1LOX

• Entry DOI: 10.2210/pdb1lox/pdb
• Descriptor: 15-LIPOXYGENASE, FE (II) ION, (2E)-3-(2-OCT-1-YN-1-YLPHENYL)ACRYLIC ACID, ... (4 entities in total)
• Functional Keywords: oxidoreductase, 15lo_depot2
• Biological source: Oryctolagus cuniculus (rabbit)
• Cellular location: Cytoplasm, cytosol : P12530
• Total number of polymer chains: 1
• Total formula weight: 75564.84

Authors

Gillmor, S.A.,Villasenor, A.,Fletterick, R.J.,Sigal, E.,Browner, M.F. (deposition date: 1997-10-06, release date: 1998-11-04, Last modification date: 2024-02-14)

Primary citation

Gillmor, S.A.,Villasenor, A.,Fletterick, R.,Sigal, E.,Browner, M.F.
The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity.
Nat.Struct.Biol., 4:1003-1009, 1997

PubMed Abstract: Here we report the first structure of a mammalian 15-lipoxygenase. The protein is composed of two domains; a catalytic domain and a previously unrecognized beta-barrel domain. The N-terminal beta-barrel domain has topological and sequence identify to a domain in the mammalian lipases, suggesting that these domains may have similar functions in vivo. Within the C-terminal domain, the lipoxygenase substrate binding site is a hydrophobic pocket defined by a bound inhibitor. Arachidonic acid can be docked into this deep hydrophobic pocket with the methyl end extending down into the bottom of the pocket and the acid end tethered by a conserved basic residue on the surface of the enzyme. This structure provides a unifying hypothesis for the positional specificity of mammalian lipoxygenases.

PubMed: 9406550
DOI: 10.1038/nsb1297-1003

Experimental method

X-RAY DIFFRACTION (2.4 Å)