1jnq

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[[Image:1jnq.jpg|left|200px]]
 
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{{Structure
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==LIPOXYGENASE-3 (SOYBEAN) COMPLEX WITH EPIGALLOCATHECHIN (EGC)==
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|PDB= 1jnq |SIZE=350|CAPTION= <scene name='initialview01'>1jnq</scene>, resolution 2.1&Aring;
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<StructureSection load='1jnq' size='340' side='right'caption='[[1jnq]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE= <scene name='pdbsite=FE:Fe+(Fe+2)+Active+Site'>FE</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=EGT:2-(3,4,5-TRIHYDROXY-PHENYL)-CHROMAN-3,5,7-TRIOL'>EGT</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>
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<table><tr><td colspan='2'>[[1jnq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JNQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JNQ FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Lipoxygenase Lipoxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] </span>
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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]] 2.1&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EGT:2-(3,4,5-TRIHYDROXY-PHENYL)-CHROMAN-3,5,7-TRIOL'>EGT</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
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|DOMAIN=
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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=1jnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jnq OCA], [https://pdbe.org/1jnq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jnq RCSB], [https://www.ebi.ac.uk/pdbsum/1jnq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jnq ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1byt|1BYT]], [[1lnh|1LNH]], [[1f8n|1F8N]], [[1lox|1LOX]], [[1ik3|1IK3]], [[1hu9|1HU9]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jnq OCA], [http://www.ebi.ac.uk/pdbsum/1jnq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jnq RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/LOX3_SOYBN LOX3_SOYBN] Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. It catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure.
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== Evolutionary Conservation ==
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'''LIPOXYGENASE-3 (SOYBEAN) COMPLEX WITH EPIGALLOCATHECHIN (EGC)'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jn/1jnq_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=1jnq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
Lipoxygenases (LOXs) are non-heme iron containing enzymes ubiquitous in nature and participating in the metabolism of the polyunsaturated fatty acids (PUFA). They are capable of combining their dioxygenase activity with its co-oxidative activity manifesting itself in biotransformation reactions catalyzed by LOXs for other than PUFA small molecules. LOXs involvement in inflammatory diseases and cancer have been well documented. Catechins are the natural flavonoids of known inhibitory activity toward dioxygenases with a potential to be utilized in disease prevention and treatment. This work presents results obtained from an X-ray analysis of (-)-epigallocatechin gallate (EGCG) interacting with soybean lipoxygenase-3. The 3D structure of the resulting complex reveals the inhibitor depicting (-)-epigallo-catechin that lacks galloyl moiety. The A-ring is near the iron co-factor, attached by the hydrogen bond to the C-terminus of the enzyme, and the B-ring hydroxyl groups participate in the hydrogen bonds and the van der Waals interactions formed by the surrounding amino acids and water molecules.
Lipoxygenases (LOXs) are non-heme iron containing enzymes ubiquitous in nature and participating in the metabolism of the polyunsaturated fatty acids (PUFA). They are capable of combining their dioxygenase activity with its co-oxidative activity manifesting itself in biotransformation reactions catalyzed by LOXs for other than PUFA small molecules. LOXs involvement in inflammatory diseases and cancer have been well documented. Catechins are the natural flavonoids of known inhibitory activity toward dioxygenases with a potential to be utilized in disease prevention and treatment. This work presents results obtained from an X-ray analysis of (-)-epigallocatechin gallate (EGCG) interacting with soybean lipoxygenase-3. The 3D structure of the resulting complex reveals the inhibitor depicting (-)-epigallo-catechin that lacks galloyl moiety. The A-ring is near the iron co-factor, attached by the hydrogen bond to the C-terminus of the enzyme, and the B-ring hydroxyl groups participate in the hydrogen bonds and the van der Waals interactions formed by the surrounding amino acids and water molecules.
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==About this Structure==
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Inhibition of lipoxygenase by (-)-epigallocatechin gallate: X-ray analysis at 2.1 A reveals degradation of EGCG and shows soybean LOX-3 complex with EGC instead.,Skrzypczak-Jankun E, Zhou K, Jankun J Int J Mol Med. 2003 Oct;12(4):415-20. PMID:12964012<ref>PMID:12964012</ref>
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1JNQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JNQ OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Inhibition of lipoxygenase by (-)-epigallocatechin gallate: X-ray analysis at 2.1 A reveals degradation of EGCG and shows soybean LOX-3 complex with EGC instead., Skrzypczak-Jankun E, Zhou K, Jankun J, Int J Mol Med. 2003 Oct;12(4):415-20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12964012 12964012]
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</div>
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<div class="pdbe-citations 1jnq" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Glycine max]]
[[Category: Glycine max]]
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[[Category: Lipoxygenase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Jankun J]]
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[[Category: Jankun, J.]]
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[[Category: Skrzypczak-Jankun E]]
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[[Category: Skrzypczak-Jankun, E.]]
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[[Category: Zhou K]]
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[[Category: Zhou, K.]]
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[[Category: catechin inhibitor]]
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[[Category: fe(ii) complex]]
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[[Category: green tea]]
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[[Category: metalloprotein]]
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[[Category: purple lipoxygenase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:36:20 2008''
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Current revision

LIPOXYGENASE-3 (SOYBEAN) COMPLEX WITH EPIGALLOCATHECHIN (EGC)

PDB ID 1jnq

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