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4e5p

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==Thermostable phosphite dehydrogenase A176R variant in complex with NAD==
==Thermostable phosphite dehydrogenase A176R variant in complex with NAD==
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<StructureSection load='4e5p' size='340' side='right' caption='[[4e5p]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='4e5p' size='340' side='right'caption='[[4e5p]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4e5p]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_stutzeri Pseudomonas stutzeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E5P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E5P FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4e5p]] 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=4E5P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E5P FirstGlance]. <br>
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</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>
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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]] 1.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4e5n|4e5n]], [[4e5k|4e5k]], [[4e5m|4e5m]]</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=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
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<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=4e5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e5p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e5p RCSB], [http://www.ebi.ac.uk/pdbsum/4e5p PDBsum]</span></td></tr>
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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=4e5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e5p OCA], [https://pdbe.org/4e5p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e5p RCSB], [https://www.ebi.ac.uk/pdbsum/4e5p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e5p ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/PTXD_PSEST PTXD_PSEST] Catalyzes phosphite (phosphonate) oxidation.
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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.
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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<ref>PMID:22564171</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Pseudomonas stutzeri]]
[[Category: Pseudomonas stutzeri]]
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[[Category: Nair, S K]]
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[[Category: Nair SK]]
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[[Category: Zhang, H]]
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[[Category: Zhang H]]
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[[Category: Zou, Y]]
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[[Category: Zou Y]]
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[[Category: D-2-hydroxyacid dehydrogenase]]
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[[Category: Oxidoreductase]]
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Current revision

Thermostable phosphite dehydrogenase A176R variant in complex with NAD

PDB ID 4e5p

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