2SBL

THE THREE-DIMENSIONAL STRUCTURE OF AN ARACHIDONIC ACID 15-LIPOXYGENASE

Summary for 2SBL

• Entry DOI: 10.2210/pdb2sbl/pdb
• Descriptor: LIPOXYGENASE-1, FE (III) ION (3 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: Glycine max (soybean)
• Cellular location: Cytoplasm: P08170
• Total number of polymer chains: 2
• Total formula weight: 189071.94

Authors

Amzel, L.M.,Boyington, J.C. (deposition date: 1993-07-22, release date: 1995-02-27, Last modification date: 2024-02-21)

Primary citation

Boyington, J.C.,Gaffney, B.J.,Amzel, L.M.
The three-dimensional structure of an arachidonic acid 15-lipoxygenase.
Science, 260:1482-1486, 1993

PubMed Abstract: In mammals, the hydroperoxidation of arachidonic acid by lipoxygenases leads to the formation of leukotrienes and lipoxins, compounds that mediate inflammatory responses. Lipoxygenases are dioxygenases that contain a nonheme iron and are present in many animal cells. Soybean lipoxygenase-1 is a single-chain, 839-residue protein closely related to mammalian lipoxygenases. The structure of soybean lipoxygenase-1 solved to 2.6 angstrom resolution shows that the enzyme has two domains: a 146-residue beta barrel and a 693-residue helical bundle. The iron atom is in the center of the larger domain and is coordinated by three histidines and the COO- of the carboxyl terminus. The coordination geometry is nonregular and appears to be a distorted octahedron in which two adjacent positions are not occupied by ligands. Two cavities, in the shapes of a bent cylinder and a frustum, connect the unoccupied positions to the surface of the enzyme. The iron, with two adjacent and unoccupied positions, is poised to interact with the 1,4-diene system of the substrate and with molecular oxygen during catalysis.

PubMed: 8502991

Experimental method

X-RAY DIFFRACTION (2.6 Å)