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| | ==SeMet thermostable phosphite dehydrogenase Glu175-Ala mutant== | | ==SeMet thermostable phosphite dehydrogenase Glu175-Ala mutant== |
| - | <StructureSection load='4ebf' size='340' side='right' caption='[[4ebf]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='4ebf' size='340' side='right'caption='[[4ebf]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ebf]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"achromobacter_sewerinii"_bergey_et_al._1923 "achromobacter sewerinii" bergey et al. 1923]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EBF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EBF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ebf]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_stutzeri Pseudomonas stutzeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EBF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EBF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4e5n|4e5n]], [[4e5k|4e5k]], [[4e5p|4e5p]], [[4e5m|4e5m]]</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=4ebf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ebf OCA], [https://pdbe.org/4ebf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ebf RCSB], [https://www.ebi.ac.uk/pdbsum/4ebf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ebf ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ptx ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=316 "Achromobacter sewerinii" Bergey et al. 1923])</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=4ebf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ebf OCA], [http://pdbe.org/4ebf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ebf RCSB], [http://www.ebi.ac.uk/pdbsum/4ebf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ebf ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PTXD_STUST PTXD_STUST] Catalyzes phosphite (phosphonate) oxidation.<ref>PMID:11278981</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Achromobacter sewerinii bergey et al. 1923]] | + | [[Category: Large Structures]] |
| - | [[Category: Nair, S K]] | + | [[Category: Pseudomonas stutzeri]] |
| - | [[Category: Zhang, H]] | + | [[Category: Nair SK]] |
| - | [[Category: Zou, Y]] | + | [[Category: Zhang H]] |
| - | [[Category: D-2-hydroxyacid dehydrogenase]] | + | [[Category: Zou Y]] |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
PTXD_STUST Catalyzes phosphite (phosphonate) oxidation.[1]
Publication Abstract from PubMed
The enzyme phosphite dehydrogenase (PTDH) catalyzes the NAD(+)-dependent conversion of phosphite to phosphate and represents the first biological catalyst that has been shown to conduct the enzymatic oxidation of phosphorus. Despite investigation for more than a decade into both the mechanism of its unusual reaction and its utility in cofactor regeneration, there has been a lack of any structural data for PTDH. Here we present the cocrystal structure of an engineered thermostable variant of PTDH bound to NAD(+) (1.7 A resolution), as well as four other cocrystal structures of thermostable PTDH and its variants with different ligands (all between 1.85 and 2.3 A resolution). These structures provide a molecular framework for understanding prior mutational analysis and point to additional residues, located in the active site, that may contribute to the enzymatic activity of this highly unusual catalyst.
Crystal structures of phosphite dehydrogenase provide insights into nicotinamide cofactor regeneration.,Zou Y, Zhang H, Brunzelle JS, Johannes TW, Woodyer R, Hung JE, Nair N, van der Donk WA, Zhao H, Nair SK Biochemistry. 2012 May 29;51(21):4263-70. Epub 2012 May 17. PMID:22564171[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Costas AM, White AK, Metcalf WW. Purification and characterization of a novel phosphorus-oxidizing enzyme from Pseudomonas stutzeri WM88. J Biol Chem. 2001 May 18;276(20):17429-36. doi: 10.1074/jbc.M011764200. Epub 2001 , Feb 22. PMID:11278981 doi:http://dx.doi.org/10.1074/jbc.M011764200
- ↑ Zou Y, Zhang H, Brunzelle JS, Johannes TW, Woodyer R, Hung JE, Nair N, van der Donk WA, Zhao H, Nair SK. Crystal structures of phosphite dehydrogenase provide insights into nicotinamide cofactor regeneration. Biochemistry. 2012 May 29;51(21):4263-70. Epub 2012 May 17. PMID:22564171 doi:10.1021/bi2016926
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