1ybv

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{{STRUCTURE_1ybv| PDB=1ybv | SCENE= }}
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==STRUCTURE OF TRIHYDROXYNAPHTHALENE REDUCTASE IN COMPLEX WITH NADPH AND AN ACTIVE SITE INHIBITOR==
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===STRUCTURE OF TRIHYDROXYNAPHTHALENE REDUCTASE IN COMPLEX WITH NADPH AND AN ACTIVE SITE INHIBITOR===
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<StructureSection load='1ybv' size='340' side='right' caption='[[1ybv]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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{{ABSTRACT_PUBMED_8939741}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ybv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Magnaporthe_grisea Magnaporthe 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YBV FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><br>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BUF+ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=148305 Magnaporthe grisea])</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tetrahydroxynaphthalene_reductase Tetrahydroxynaphthalene reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.252 1.1.1.252] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ybv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ybv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ybv RCSB], [http://www.ebi.ac.uk/pdbsum/1ybv PDBsum]</span></td></tr>
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<table>
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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/yb/1ybv_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/chain_selection.php?pdb_ID=2ata 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 ==
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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. Tricyclazole, an inhibitor of the enzyme, binds at the active site in the vicinity of the NADPH nicotinamide ring. The active site contains a Ser-Tyr-Lys triad which is proposed to participate in catalysis. Coenzyme specificity is partly conferred by the interaction of a single basic residue, Arg39, with the 2' phosphate group of NADPH. CONCLUSIONS: The structural model reveals THNR to belong to the family of short chain dehydrogenases. Despite the diversity of the chemical reactions catalyzed by this family of enzymes, their tertiary structures are very similar. In particular THNR has many amino acid sequence identities, and thus most probably high structural similarities, to enzymes involved in fungal aflatoxin synthesis. The structure of THNR in complex with NADPH and tricyclazole provides new insights into the structural basis of inhibitor binding. This new information may aid in the design of new inhibitors for rice crop protection.
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==About this Structure==
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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:8939741<ref>PMID:8939741</ref>
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[[1ybv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Magnaporthe_grisea Magnaporthe grisea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YBV OCA].
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
==See Also==
==See Also==
*[[InhA|InhA]]
*[[InhA|InhA]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:008939741</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Magnaporthe grisea]]
[[Category: Magnaporthe grisea]]
[[Category: Tetrahydroxynaphthalene reductase]]
[[Category: Tetrahydroxynaphthalene reductase]]

Revision as of 21:29, 29 September 2014

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

1ybv, resolution 2.80Å

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