1lox

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[[Image:1lox.gif|left|200px]]<br />
 
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<applet load="1lox" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1lox, resolution 2.4&Aring;" />
 
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'''RABBIT RETICULOCYTE 15-LIPOXYGENASE'''<br />
 
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==Overview==
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==RABBIT RETICULOCYTE 15-LIPOXYGENASE==
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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.
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<StructureSection load='1lox' size='340' side='right'caption='[[1lox]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1lox]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LOX FirstGlance]. <br>
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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 FE2 and RS7 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] Structure known Active Site: NUL. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LOX OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lox OCA], [https://pdbe.org/1lox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lox RCSB], [https://www.ebi.ac.uk/pdbsum/1lox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lox ProSAT]</span></td></tr>
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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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</table>
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[[Category: Arachidonate 15-lipoxygenase]]
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== Function ==
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[https://www.uniprot.org/uniprot/LOX15_RABIT LOX15_RABIT]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lo/1lox_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lox ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Single protein]]
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[[Category: Browner MF]]
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[[Category: Browner, M.F.]]
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[[Category: Fletterick RJ]]
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[[Category: Fletterick, R.J.]]
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[[Category: Gillmor SA]]
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[[Category: Gillmor, S.A.]]
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[[Category: Sigal E]]
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[[Category: Sigal, E.]]
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[[Category: Villasenor A]]
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[[Category: Villasenor, A.]]
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[[Category: FE2]]
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[[Category: RS7]]
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[[Category: 15lo_depot2]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:59:51 2007''
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Current revision

RABBIT RETICULOCYTE 15-LIPOXYGENASE

PDB ID 1lox

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