1doh

<StructureSection load='1doh' size='340' side='right' caption='[[1doh]], [[Resolution|resolution]] 2.10&Aring;' scene=''>

<table><tr><td colspan='2'>[[1doh]] 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=1DOH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DOH FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=NID:4-NITRO-INDEN-1-ONE'>NID</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ybv|1ybv]]</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1doh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1doh OCA], [http://pdbe.org/1doh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1doh RCSB], [http://www.ebi.ac.uk/pdbsum/1doh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1doh ProSAT]</span></td></tr>

[[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.

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== Publication Abstract from PubMed ==

BACKGROUND: Trihydroxynaphthalene reductase catalyzes two intermediate steps in the fungal melanin biosynthetic pathway. The enzyme, a typical short-chain dehydrogenase, is the biochemical target of three commercial fungicides. The fungicides bind preferentially to the NADPH form of the enzyme. RESULTS: Three X-ray structures of the Magnaporthe grisea enzyme complexed with NADPH and two commercial and one experimental fungicide were determined at 1.7 A (pyroquilon), 2.0 A (2,3-dihydro-4-nitro-1H-inden-1-one, 1), and 2.1 A (phthalide) resolutions. The chemically distinct inhibitors occupy similar space within the enzyme's active site. The three inhibitors share hydrogen bonds with the side chain hydroxyls of Ser-164 and Tyr-178 via a carbonyl oxygen (pyroquilon and 1) or via a carbonyl oxygen and a ring oxygen (phthalide). Active site residues occupy similar positions among the three structures. A buried water molecule that is hydrogen bonded to the NZ nitrogen of Lys-182 in each of the three structures likely serves to stabilize the cationic form of the residue for participation in catalysis. CONCLUSIONS: The pro S hydrogen of NADPH (which is transferred as a hydride to the enzyme's naphthol substrates) is directed toward the carbonyl carbon of the inhibitors that mimic an intermediate along the reaction coordinate. Modeling tetrahydroxynaphthalene and trihydroxynaphthalene in the active site shows steric and electrostatic repulsion between the extra hydroxyl oxygen of the former substrate and the sulfur atom of Met-283 (the C-terminal residue), which accounts, in part, for the 4-fold greater substrate specificity for trihydroxynaphthalene over tetrahydroxynaphthalene.

Structures of trihydroxynaphthalene reductase-fungicide complexes: implications for structure-based design and catalysis.,Liao D, Basarab GS, Gatenby AA, Valent B, Jordan DB Structure. 2001 Jan 10;9(1):19-27. PMID:11342131<ref>PMID:11342131</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1doh" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Tetrahydroxynaphthalene reductase]]

[[Category: Basarab, G S]]

[[Category: Gatenby, A A]]

[[Category: Jordan, D B]]

[[Category: Liao, D I]]

[[Category: Dinucleotide binding fold]]

[[Category: Protein-nadph-active site inhibitor complex]]