 |
PDBsum entry 2sbl
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Oxidoreductase
|
PDB id
|
|
|
|
2sbl
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
The three-Dimensional structure of an arachidonic acid 15-Lipoxygenase.
|
|
|
Authors
|
|
J.C.Boyington,
B.J.Gaffney,
L.M.Amzel.
|
|
|
Ref.
|
|
Science, 1993,
260,
1482-1486.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Crystallization and preliminary X-Ray analysis of soybean lipoxygenase-1, A non-Heme iron-Containing dioxygenase.
|
|
|
Authors
|
|
J.C.Boyington,
B.J.Gaffney,
L.M.Amzel.
|
|
|
Ref.
|
|
J Biol Chem, 1990,
265,
12771-12773.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
