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1lox

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[[Image:1lox.gif|left|200px]]<br /><applet load="1lox" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1lox.gif|left|200px]]
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caption="1lox, resolution 2.4&Aring;" />
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'''RABBIT RETICULOCYTE 15-LIPOXYGENASE'''<br />
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{{Structure
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|PDB= 1lox |SIZE=350|CAPTION= <scene name='initialview01'>1lox</scene>, resolution 2.4&Aring;
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|SITE= <scene name='pdbsite=NUL:Catalytic+Fe+And+Its+Ligands'>NUL</scene>
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|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>
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|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]
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|GENE=
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}}
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'''RABBIT RETICULOCYTE 15-LIPOXYGENASE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1LOX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=FE2:'>FE2</scene> and <scene name='pdbligand=RS7:'>RS7</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=NUL:Catalytic+Fe+And+Its+Ligands'>NUL</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LOX OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9406550 9406550]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:00 2008''
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''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


PDB ID 1lox

Drag the structure with the mouse to rotate
, 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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