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Title:
The Three-Dimensional Structure of an Arachidonic Acid 15-Lipoxygenase
Authors:
Boyington, Jeffrey C.; Gaffney, Betty J.; Amzel, L. Mario
Publication:
Science, Volume 260, Issue 5113, pp. 1482-1486 (Sci Homepage)
Publication Date:
06/1993
Origin:
JSTOR
DOI:
10.1126/science.8502991
Bibliographic Code:
1993Sci...260.1482B

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 β 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.
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