2sbl
From Proteopedia
(New page: 200px<br /><applet load="2sbl" size="450" color="white" frame="true" align="right" spinBox="true" caption="2sbl, resolution 2.6Å" /> '''THE THREE-DIMENSIONAL...) |
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| - | [[Image:2sbl.jpg|left|200px]]<br /><applet load="2sbl" size=" | + | [[Image:2sbl.jpg|left|200px]]<br /><applet load="2sbl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2sbl, resolution 2.6Å" /> | caption="2sbl, resolution 2.6Å" /> | ||
'''THE THREE-DIMENSIONAL STRUCTURE OF AN ARACHIDONIC ACID 15-LIPOXYGENASE'''<br /> | '''THE THREE-DIMENSIONAL STRUCTURE OF AN ARACHIDONIC ACID 15-LIPOXYGENASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In mammals, the hydroperoxidation of arachidonic acid by lipoxygenases | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2SBL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max] with FE as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Lipoxygenase Lipoxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] Full crystallographic information is available from [http:// | + | 2SBL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max] with <scene name='pdbligand=FE:'>FE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Lipoxygenase Lipoxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SBL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Lipoxygenase]] | [[Category: Lipoxygenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Amzel, L | + | [[Category: Amzel, L M.]] |
| - | [[Category: Boyington, J | + | [[Category: Boyington, J C.]] |
[[Category: FE]] | [[Category: FE]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:49:06 2008'' |
Revision as of 16:49, 21 February 2008
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THE THREE-DIMENSIONAL STRUCTURE OF AN ARACHIDONIC ACID 15-LIPOXYGENASE
Overview
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.
About this Structure
2SBL is a Single protein structure of sequence from Glycine max with as ligand. Active as Lipoxygenase, with EC number 1.13.11.12 Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of an arachidonic acid 15-lipoxygenase., Boyington JC, Gaffney BJ, Amzel LM, Science. 1993 Jun 4;260(5113):1482-6. PMID:8502991
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