1nas

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(New page: 200px<br /><applet load="1nas" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nas, resolution 2.1&Aring;" /> '''SEPIAPTERIN REDUCTASE...)
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[[Image:1nas.gif|left|200px]]<br /><applet load="1nas" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1nas, resolution 2.1&Aring;" />
 
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'''SEPIAPTERIN REDUCTASE COMPLEXED WITH N-ACETYL SEROTONIN'''<br />
 
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==Overview==
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==SEPIAPTERIN REDUCTASE COMPLEXED WITH N-ACETYL SEROTONIN==
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Sepiapterin reductase catalyses the last steps in the biosynthesis of, tetrahydrobiopterin, the essential co-factor of aromatic amino acid, hydroxylases and nitric oxide synthases. We have determined the crystal, structure of mouse sepiapterin reductase by multiple isomorphous, replacement at a resolution of 1.25 A in its ternary complex with, oxaloacetate and NADP. The homodimeric structure reveals a single-domain, alpha/beta-fold with a central four-helix bundle connecting two, seven-stranded parallel beta-sheets, each sandwiched between two arrays of, three helices. Ternary complexes with the substrate sepiapterin or the, product tetrahydrobiopterin were studied. Each subunit contains a specific, aspartate anchor (Asp258) for pterin-substrates, which positions the, substrate side chain C1'-carbonyl group near Tyr171 OH and NADP C4'N. The, catalytic mechanism of SR appears to consist of a NADPH-dependent proton, transfer from Tyr171 to the substrate C1' and C2' carbonyl functions, accompanied by stereospecific side chain isomerization. Complex structures, with the inhibitor N-acetyl serotonin show the indoleamine bound such that, both reductase and isomerase activity for pterins is inhibited, but, reaction with a variety of carbonyl compounds is possible. The complex, structure with N-acetyl serotonin suggests the possibility for a highly, specific feedback regulatory mechanism between the formation of, indoleamines and pteridines in vivo.
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<StructureSection load='1nas' size='340' side='right'caption='[[1nas]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1nas]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NAS FirstGlance]. <br>
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1NAS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with OAA, NAP and ASE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Sepiapterin_reductase Sepiapterin reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.153 1.1.1.153] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NAS 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]] 2.1&#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=ASE:N-ACETYL+SEROTONIN'>ASE</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</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=1nas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nas OCA], [https://pdbe.org/1nas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nas RCSB], [https://www.ebi.ac.uk/pdbsum/1nas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nas ProSAT]</span></td></tr>
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The 1.25 A crystal structure of sepiapterin reductase reveals its binding mode to pterins and brain neurotransmitters., Auerbach G, Herrmann A, Gutlich M, Fischer M, Jacob U, Bacher A, Huber R, EMBO J. 1997 Dec 15;16(24):7219-30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9405351 9405351]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SPRE_MOUSE SPRE_MOUSE] Catalyzes the final one or two reductions in tetra-hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin.
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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/na/1nas_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/main_output.php?pdb_ID=1nas 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]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Sepiapterin reductase]]
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[[Category: Auerbach G]]
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[[Category: Single protein]]
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[[Category: Bacher A]]
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[[Category: Auerbach, G.]]
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[[Category: Herrmann A]]
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[[Category: Bacher, A.]]
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[[Category: Huber R]]
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[[Category: Herrmann, A.]]
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[[Category: Huber, R.]]
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[[Category: ASE]]
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[[Category: NAP]]
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[[Category: OAA]]
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[[Category: n-acetyl serotonin]]
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[[Category: oxidoreductase]]
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[[Category: sdr family]]
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[[Category: sepiapterin reductase]]
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[[Category: short-chain dehydrogenase]]
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[[Category: tetrahydrobiopterin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:06:11 2007''
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Current revision

SEPIAPTERIN REDUCTASE COMPLEXED WITH N-ACETYL SEROTONIN

PDB ID 1nas

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