1lox: Difference between revisions
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[[Image:1lox.gif|left|200px]] | [[Image:1lox.gif|left|200px]] | ||
'''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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| 1lox, resolution 2.4Å | |||||||||||||
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| Sites: | NUL | ||||||||||||
| Ligands: | FE2 and RS7 | ||||||||||||
| 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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