View source for 5voh


==Crystal structure of engineered water-forming NADPH oxidase (TPNOX) bound to NADPH. The G159A, D177A, A178R, M179S, P184R mutant of LbNOX.==
<StructureSection load='5voh' size='340' side='right'caption='[[5voh]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5voh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Levilactobacillus_brevis_KB290 Levilactobacillus brevis KB290]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VOH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.302&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5voh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5voh OCA], [https://pdbe.org/5voh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5voh RCSB], [https://www.ebi.ac.uk/pdbsum/5voh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5voh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/M5B0V2_LEVBR M5B0V2_LEVBR] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The redox coenzymes NADH and NADPH are broadly required for energy metabolism, biosynthesis and detoxification. Despite detailed knowledge of specific enzymes and pathways that utilize these coenzymes, a holistic understanding of the regulation and compartmentalization of NADH- and NADPH-dependent pathways is lacking, partly because of a lack of tools with which to investigate these processes in living cells. We have previously reported the use of the naturally occurring Lactobacillus brevis H2O-forming NADH oxidase (LbNOX) as a genetic tool for manipulation of the NAD+/NADH ratio in human cells. Here, we present triphosphopyridine nucleotide oxidase (TPNOX), a rationally designed and engineered mutant of LbNOX that is strictly specific to NADPH. We characterized the effects of TPNOX expression on cellular metabolism and used it in combination with LbNOX to show how the redox states of mitochondrial NADPH and NADH pools are connected.

A genetically encoded tool for manipulation of NADP+/NADPH in living cells.,Cracan V, Titov DV, Shen H, Grabarek Z, Mootha VK Nat Chem Biol. 2017 Aug 7. doi: 10.1038/nchembio.2454. PMID:28805804<ref>PMID:28805804</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5voh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Levilactobacillus brevis KB290]]
[[Category: Cracan V]]
[[Category: Grabarek Z]]