1lox
From Proteopedia
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| - | [[Image:1lox.gif|left|200px]] | + | [[Image:1lox.gif|left|200px]] |
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| - | '''RABBIT RETICULOCYTE 15-LIPOXYGENASE''' | + | {{Structure |
| + | |PDB= 1lox |SIZE=350|CAPTION= <scene name='initialview01'>1lox</scene>, resolution 2.4Å | ||
| + | |SITE= <scene name='pdbsite=NUL:Catalytic+Fe+And+Its+Ligands'>NUL</scene> | ||
| + | |LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene> and <scene name='pdbligand=RS7:(2E)-3-(2-OCT-1-YN-1-YLPHENYL)ACRYLIC ACID'>RS7</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Arachidonate_15-lipoxygenase Arachidonate 15-lipoxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.33 1.13.11.33] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''RABBIT RETICULOCYTE 15-LIPOXYGENASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LOX is a [ | + | 1LOX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LOX OCA]. |
==Reference== | ==Reference== | ||
| - | The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity., Gillmor SA, Villasenor A, Fletterick R, Sigal E, Browner MF, Nat Struct Biol. 1997 Dec;4(12):1003-9. PMID:[http:// | + | The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity., Gillmor SA, Villasenor A, Fletterick R, Sigal E, Browner MF, Nat Struct Biol. 1997 Dec;4(12):1003-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9406550 9406550] |
[[Category: Arachidonate 15-lipoxygenase]] | [[Category: Arachidonate 15-lipoxygenase]] | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:33:24 2008'' |
Revision as of 10:33, 20 March 2008
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| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | and | ||||||
| Activity: | Arachidonate 15-lipoxygenase, with EC number 1.13.11.33 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
RABBIT RETICULOCYTE 15-LIPOXYGENASE
Overview
Here we report the first structure of a mammalian 15-lipoxygenase. The protein is composed of two domains; a catalytic domain and a previously unrecognized beta-barrel domain. The N-terminal beta-barrel domain has topological and sequence identify to a domain in the mammalian lipases, suggesting that these domains may have similar functions in vivo. Within the C-terminal domain, the lipoxygenase substrate binding site is a hydrophobic pocket defined by a bound inhibitor. Arachidonic acid can be docked into this deep hydrophobic pocket with the methyl end extending down into the bottom of the pocket and the acid end tethered by a conserved basic residue on the surface of the enzyme. This structure provides a unifying hypothesis for the positional specificity of mammalian lipoxygenases.
About this Structure
1LOX is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity., Gillmor SA, Villasenor A, Fletterick R, Sigal E, Browner MF, Nat Struct Biol. 1997 Dec;4(12):1003-9. PMID:9406550
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