1ybv

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[[Image:1ybv.gif|left|200px]]<br />
 
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<applet load="1ybv" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ybv, resolution 2.8&Aring;" />
 
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'''STRUCTURE OF TRIHYDROXYNAPHTHALENE REDUCTASE IN COMPLEX WITH NADPH AND AN ACTIVE SITE INHIBITOR'''<br />
 
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==Overview==
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==STRUCTURE OF TRIHYDROXYNAPHTHALENE REDUCTASE IN COMPLEX WITH NADPH AND AN ACTIVE SITE INHIBITOR==
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BACKGROUND: The enzyme 1,3,8-trihydroxynaphthalene reductase (THNR), catalyzes an essential reaction in the biosynthesis of melanin, a black, pigment crucial for the pathogenesis of the rice blast fungus, Magnaporthe, grisea. The enzyme is the biochemical target of several commercially, important fungicides which are used to prevent blast disease in rice, plants. We have determined the structure of the ternary complex of THNR, with bound NADPH and a fungicide, tricyclazole. RESULTS: Crystallographic, analysis showed four identical subunits of THNR to form a tetramer with, 222 symmetry. The enzyme subunit consists of a single domain comprising a, seven-stranded beta sheet flanked by eight alpha helices; the subunit, contains a dinucleotide-binding fold which binds the coenzyme, NADPH., ... [[http://ispc.weizmann.ac.il/pmbin/getpm?8939741 (full description)]]
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<StructureSection load='1ybv' size='340' side='right'caption='[[1ybv]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1ybv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyricularia_grisea Pyricularia grisea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YBV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YBV FirstGlance]. <br>
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1YBV is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Magnaporthe_grisea Magnaporthe grisea]] with NDP and BEA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Transferred_entry:_1.1.1.252 Transferred entry: 1.1.1.252]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.50 1.3.1.50]]. Structure known Active Sites: A1, A2, B1 and B2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YBV 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]] 2.8&#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=BEA:5-METHYL-1,2,4-TRIAZOLO[3,4-B]BENZOTHIAZOLE'>BEA</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</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=1ybv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ybv OCA], [https://pdbe.org/1ybv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ybv RCSB], [https://www.ebi.ac.uk/pdbsum/1ybv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ybv ProSAT]</span></td></tr>
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Crystal structure of the ternary complex of 1,3,8-trihydroxynaphthalene reductase from Magnaporthe grisea with NADPH and an active-site inhibitor., Andersson A, Jordan D, Schneider G, Lindqvist Y, Structure. 1996 Oct 15;4(10):1161-70. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8939741 8939741]
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</table>
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[[Category: Magnaporthe grisea]]
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== Function ==
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[[Category: Single protein]]
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[https://www.uniprot.org/uniprot/T4HR_MAGO7 T4HR_MAGO7] Catalyzes the NADPH-dependent reduction of 1,3,6,8-tetrahydroxynaphthalene (T4HN) into (+)-scytalone and 1,3,8-trihydroxynaphthalene into (-)-vermelone. This enzyme is the biochemical target of several commercially important fungicides which are used to prevent blast disease in rice plants.
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[[Category: Transferred entry: 1.1.1.252]]
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== Evolutionary Conservation ==
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[[Category: Andersson, A.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Lindqvist, Y.]]
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Check<jmol>
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[[Category: Schneider, G.]]
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<jmolCheckbox>
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[[Category: BEA]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yb/1ybv_consurf.spt"</scriptWhenChecked>
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[[Category: NDP]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: oxidoreductase]]
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:33:15 2007''
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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=1ybv 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]]
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[[Category: Pyricularia grisea]]
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[[Category: Andersson A]]
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[[Category: Lindqvist Y]]
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[[Category: Schneider G]]

Current revision

STRUCTURE OF TRIHYDROXYNAPHTHALENE REDUCTASE IN COMPLEX WITH NADPH AND AN ACTIVE SITE INHIBITOR

PDB ID 1ybv

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