5vn0
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Water-forming NADH oxidase from Lactobacillus brevis (LbNOX) bound to NADH.== | |
| + | <StructureSection load='5vn0' size='340' side='right'caption='[[5vn0]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5vn0]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Levilactobacillus_brevis_ATCC_367 Levilactobacillus brevis ATCC 367]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VN0 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]] 2.001Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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=5vn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vn0 OCA], [https://pdbe.org/5vn0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vn0 RCSB], [https://www.ebi.ac.uk/pdbsum/5vn0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vn0 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q03Q85_LEVBA Q03Q85_LEVBA] | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Cracan | + | <div class="pdbe-citations 5vn0" style="background-color:#fffaf0;"></div> |
| - | [[Category: Grabarek | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Levilactobacillus brevis ATCC 367]] | ||
| + | [[Category: Cracan V]] | ||
| + | [[Category: Grabarek Z]] | ||
Current revision
Water-forming NADH oxidase from Lactobacillus brevis (LbNOX) bound to NADH.
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