2sbl: Difference between revisions

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[[Image:2sbl.jpg|left|200px]]
{{Seed}}
[[Image:2sbl.png|left|200px]]


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{{STRUCTURE_2sbl|  PDB=2sbl  |  SCENE=  }}  
{{STRUCTURE_2sbl|  PDB=2sbl  |  SCENE=  }}  


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




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_8502991}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_8502991}}


==About this Structure==
==About this Structure==
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[[Category: Boyington, J C.]]
[[Category: Boyington, J C.]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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