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1g0n

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(New page: 200px<br /><applet load="1g0n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g0n, resolution 2.0&Aring;" /> '''STRUCTURE OF TRIHYDRO...)
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[[Image:1g0n.jpg|left|200px]]<br /><applet load="1g0n" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1g0n, resolution 2.0&Aring;" />
 
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'''STRUCTURE OF TRIHYDROXYNAPHTHALENE REDUCTASE IN COMPLEX WITH NADPH AND 4,5,6,7-TETRACHLORO-PHTHALIDE'''<br />
 
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==Overview==
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==STRUCTURE OF TRIHYDROXYNAPHTHALENE REDUCTASE IN COMPLEX WITH NADPH AND 4,5,6,7-TETRACHLORO-PHTHALIDE==
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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.
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<StructureSection load='1g0n' size='340' side='right'caption='[[1g0n]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1g0n]] 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=1G0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G0N FirstGlance]. <br>
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1G0N 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 PHH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G0N 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&#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=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=PHH:4,5,6,7-TETRACHLORO-PHTHALIDE'>PHH</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=1g0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g0n OCA], [https://pdbe.org/1g0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g0n RCSB], [https://www.ebi.ac.uk/pdbsum/1g0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g0n ProSAT]</span></td></tr>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11342131 11342131]
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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: Tetrahydroxynaphthalene reductase]]
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== Evolutionary Conservation ==
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[[Category: Basarab, G.S.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Gatenby, A.A.]]
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Check<jmol>
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[[Category: Jordan, D.B.]]
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<jmolCheckbox>
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[[Category: Liao, D.]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g0/1g0n_consurf.spt"</scriptWhenChecked>
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[[Category: Valent, B.]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: NDP]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: PHH]]
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</jmolCheckbox>
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[[Category: diuncleotide binding fold]]
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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=1g0n ConSurf].
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[[Category: oxidoreductase]]
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<div style="clear:both"></div>
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[[Category: protein-nadph-active site inhibitor complex]]
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__TOC__
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[[Category: short chain dehydrogenase]]
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</StructureSection>
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[[Category: Large Structures]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:35:38 2007''
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[[Category: Pyricularia grisea]]
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[[Category: Basarab GS]]
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[[Category: Gatenby AA]]
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[[Category: Jordan DB]]
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[[Category: Liao D]]
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[[Category: Valent B]]

Current revision

STRUCTURE OF TRIHYDROXYNAPHTHALENE REDUCTASE IN COMPLEX WITH NADPH AND 4,5,6,7-TETRACHLORO-PHTHALIDE

PDB ID 1g0n

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