4e5m: Difference between revisions

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<StructureSection load='4e5m' size='340' side='right'caption='[[4e5m]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='4e5m' size='340' side='right'caption='[[4e5m]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4e5m]] is a 2 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=4E5M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E5M FirstGlance]. <br>
<table><tr><td colspan='2'>[[4e5m]] is a 2 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=4E5M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E5M FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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]] 1.85&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4e5k|4e5k]], [[4e5n|4e5n]], [[4e5p|4e5p]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></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=4e5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e5m OCA], [http://pdbe.org/4e5m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e5m RCSB], [http://www.ebi.ac.uk/pdbsum/4e5m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4e5m 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=4e5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e5m OCA], [https://pdbe.org/4e5m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e5m RCSB], [https://www.ebi.ac.uk/pdbsum/4e5m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e5m ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/PTXD_PSEST PTXD_PSEST] Catalyzes phosphite (phosphonate) oxidation.
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<ref>PMID:22564171</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4e5m" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Achromobacter sewerinii bergey et al. 1923]]
[[Category: Large Structures]]
[[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]]

Latest revision as of 11:01, 1 March 2024

Thermostable phosphite dehydrogenase E175A/A176R in complex with NADP

4e5m, resolution 1.85Å

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