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| | <StructureSection load='1ybv' size='340' side='right'caption='[[1ybv]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='1ybv' size='340' side='right'caption='[[1ybv]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ybv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_138707_[[pyricularia_grisea]] Cbs 138707 [[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 [http://proteopedia.org/fgij/fg.htm?mol=1YBV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ybv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpi_625033_[[magnaporthe_grisea]] Bpi 625033 [[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 [https://proteopedia.org/fgij/fg.htm?mol=1YBV FirstGlance]. <br> |
| | </td></tr><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> | | </td></tr><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> |
| - | <tr id='gene'><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 CBS 138707 [[Pyricularia grisea]]])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BUF+ ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=148305 BPI 625033 [[Magnaporthe grisea]]])</td></tr> |
| - | <tr id='activity'><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> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Tetrahydroxynaphthalene_reductase Tetrahydroxynaphthalene reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.252 1.1.1.252] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ybv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ybv OCA], [http://pdbe.org/1ybv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ybv RCSB], [http://www.ebi.ac.uk/pdbsum/1ybv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ybv ProSAT]</span></td></tr> | + | <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> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [[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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1ybv" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1ybv" style="background-color:#fffaf0;"></div> |
| - | | |
| - | ==See Also== | |
| - | *[[InhA|InhA]] | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Structural highlights
Function
[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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Andersson A, Jordan D, Schneider G, Lindqvist Y. Crystal structure of the ternary complex of 1,3,8-trihydroxynaphthalene reductase from Magnaporthe grisea with NADPH and an active-site inhibitor. Structure. 1996 Oct 15;4(10):1161-70. PMID:8939741
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