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4o9u

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==Mechanism of transhydrogenase coupling proton translocation and hydride transfer==
==Mechanism of transhydrogenase coupling proton translocation and hydride transfer==
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<StructureSection load='4o9u' size='340' side='right' caption='[[4o9u]], [[Resolution|resolution]] 6.93&Aring;' scene=''>
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<StructureSection load='4o9u' size='340' side='right'caption='[[4o9u]], [[Resolution|resolution]] 6.93&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4o9u]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O9U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O9U FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4o9u]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O9U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O9U 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>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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]] 6.926&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(Re/Si-specific) NAD(P)(+) transhydrogenase (Re/Si-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.2 1.6.1.2] </span></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>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=4o9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o9u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o9u RCSB], [http://www.ebi.ac.uk/pdbsum/4o9u 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=4o9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o9u OCA], [https://pdbe.org/4o9u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o9u RCSB], [https://www.ebi.ac.uk/pdbsum/4o9u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o9u ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/Q72GS0_THET2 Q72GS0_THET2]] The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane (By similarity).[PIRNR:PIRNR000204]
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[https://www.uniprot.org/uniprot/Q72GR9_THET2 Q72GR9_THET2]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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NADPH/NADP(+) (the reduced form of NADP(+)/nicotinamide adenine dinucleotide phosphate) homeostasis is critical for countering oxidative stress in cells. Nicotinamide nucleotide transhydrogenase (TH), a membrane enzyme present in both bacteria and mitochondria, couples the proton motive force to the generation of NADPH. We present the 2.8 A crystal structure of the transmembrane proton channel domain of TH from Thermus thermophilus and the 6.9 A crystal structure of the entire enzyme (holo-TH). The membrane domain crystallized as a symmetric dimer, with each protomer containing a putative proton channel. The holo-TH is a highly asymmetric dimer with the NADP(H)-binding domain (dIII) in two different orientations. This unusual arrangement suggests a catalytic mechanism in which the two copies of dIII alternatively function in proton translocation and hydride transfer.
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Structural biology. Division of labor in transhydrogenase by alternating proton translocation and hydride transfer.,Leung JH, Schurig-Briccio LA, Yamaguchi M, Moeller A, Speir JA, Gennis RB, Stout CD Science. 2015 Jan 9;347(6218):178-81. doi: 10.1126/science.1260451. PMID:25574024<ref>PMID:25574024</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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==See Also==
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</div>
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*[[NAD(P) transhydrogenase 3D structures|NAD(P) transhydrogenase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Carragher, B]]
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[[Category: Large Structures]]
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[[Category: Gennis, R B]]
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[[Category: Thermus thermophilus HB27]]
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[[Category: Leung, J H]]
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[[Category: Carragher B]]
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[[Category: Moeller, A]]
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[[Category: Gennis RB]]
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[[Category: Potter, C S]]
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[[Category: Leung JH]]
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[[Category: Schurig-Briccio, L A]]
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[[Category: Moeller A]]
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[[Category: Stout, C D]]
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[[Category: Potter CS]]
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[[Category: Yamaguchi, M]]
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[[Category: Schurig-Briccio LA]]
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[[Category: Alpha2]]
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[[Category: Stout CD]]
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[[Category: And domain iii as a dimer]]
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[[Category: Yamaguchi M]]
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[[Category: Couples proton motive]]
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[[Category: Holo-transhydrogease from thermus thermophilus assembled from subunits alpha1]]
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[[Category: Hydride transfer]]
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[[Category: Membrane protein]]
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[[Category: Nicotinamide nucleotide transhydrogenase]]
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[[Category: Periplasmic membrane and cytosol]]
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[[Category: Proton translocation and hydride transfer]]
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[[Category: Truncated beta]]
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Current revision

Mechanism of transhydrogenase coupling proton translocation and hydride transfer

PDB ID 4o9u

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