1lox

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[[Image:1lox.gif|left|200px]]
[[Image:1lox.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1lox |SIZE=350|CAPTION= <scene name='initialview01'>1lox</scene>, resolution 2.4&Aring;
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The line below this paragraph, containing "STRUCTURE_1lox", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=NUL:Catalytic+Fe+And+Its+Ligands'>NUL</scene>
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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=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=RS7:(2E)-3-(2-OCT-1-YN-1-YLPHENYL)ACRYLIC+ACID'>RS7</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/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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1lox| PDB=1lox | 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=1lox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lox OCA], [http://www.ebi.ac.uk/pdbsum/1lox PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lox RCSB]</span>
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}}
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'''RABBIT RETICULOCYTE 15-LIPOXYGENASE'''
'''RABBIT RETICULOCYTE 15-LIPOXYGENASE'''
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[[Category: Villasenor, A.]]
[[Category: Villasenor, A.]]
[[Category: 15lo_depot2]]
[[Category: 15lo_depot2]]
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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 Sat May 3 00:07:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:05:29 2008''
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Revision as of 21:07, 2 May 2008

Image:1lox.gif

Template:STRUCTURE 1lox

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 Page seeded by OCA on Sat May 3 00:07:57 2008

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