1nas: Difference between revisions
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<StructureSection load='1nas' size='340' side='right'caption='[[1nas]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1nas' size='340' side='right'caption='[[1nas]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1nas]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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> | ||
</td></tr><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><tr id='method'><td class="sblockLbl"><b>[[Method|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction</td></tr> | ||
<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> | |||
<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> | <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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Auerbach | [[Category: Auerbach G]] | ||
[[Category: Bacher | [[Category: Bacher A]] | ||
[[Category: Herrmann | [[Category: Herrmann A]] | ||
[[Category: Huber | [[Category: Huber R]] | ||
Revision as of 21:53, 28 June 2023
SEPIAPTERIN REDUCTASE COMPLEXED WITH N-ACETYL SEROTONINSEPIAPTERIN REDUCTASE COMPLEXED WITH N-ACETYL SEROTONIN
Structural highlights
FunctionSPRE_MOUSE Catalyzes the final one or two reductions in tetra-hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin. 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 PubMedSepiapterin 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. 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:9405351[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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