2sbl

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[[Image:2sbl.jpg|left|200px]]
[[Image:2sbl.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2sbl |SIZE=350|CAPTION= <scene name='initialview01'>2sbl</scene>, resolution 2.6&Aring;
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The line below this paragraph, containing "STRUCTURE_2sbl", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_2sbl| PDB=2sbl | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2sbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2sbl OCA], [http://www.ebi.ac.uk/pdbsum/2sbl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2sbl RCSB]</span>
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}}
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'''THE THREE-DIMENSIONAL STRUCTURE OF AN ARACHIDONIC ACID 15-LIPOXYGENASE'''
'''THE THREE-DIMENSIONAL STRUCTURE OF AN ARACHIDONIC ACID 15-LIPOXYGENASE'''
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[[Category: Amzel, L M.]]
[[Category: Amzel, L M.]]
[[Category: Boyington, J C.]]
[[Category: Boyington, J C.]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:17:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:02:50 2008''
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Revision as of 14:17, 4 May 2008

Image:2sbl.jpg

Template:STRUCTURE 2sbl

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. 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 Page seeded by OCA on Sun May 4 17:17:28 2008

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