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| | <StructureSection load='4o93' size='340' side='right'caption='[[4o93]], [[Resolution|resolution]] 2.77Å' scene=''> | | <StructureSection load='4o93' size='340' side='right'caption='[[4o93]], [[Resolution|resolution]] 2.77Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4o93]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet2 Thet2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O93 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O93 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4o93]] is a 4 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=4O93 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O93 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</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]] 2.77Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TT_C1779 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2]), TT_C1778 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr> |
| - | <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> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o93 OCA], [https://pdbe.org/4o93 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o93 RCSB], [https://www.ebi.ac.uk/pdbsum/4o93 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o93 ProSAT]</span></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=4o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o93 OCA], [http://pdbe.org/4o93 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o93 RCSB], [http://www.ebi.ac.uk/pdbsum/4o93 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o93 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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] | + | [https://www.uniprot.org/uniprot/Q72GR9_THET2 Q72GR9_THET2] |
| - | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 4o93" style="background-color:#fffaf0;"></div>
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[NAD(P) transhydrogenase|NAD(P) transhydrogenase]] | + | *[[NAD(P) transhydrogenase 3D structures|NAD(P) transhydrogenase 3D structures]] |
| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thet2]] | + | [[Category: Thermus thermophilus HB27]] |
| - | [[Category: Carragher, B]] | + | [[Category: Carragher B]] |
| - | [[Category: Gennis, R B]] | + | [[Category: Gennis RB]] |
| - | [[Category: Leung, J H]] | + | [[Category: Leung JH]] |
| - | [[Category: Moeller, A]] | + | [[Category: Moeller A]] |
| - | [[Category: Potter, C S]] | + | [[Category: Potter CS]] |
| - | [[Category: Schurig-Briccio, L A]] | + | [[Category: Schurig-Briccio LA]] |
| - | [[Category: Stout, C D]] | + | [[Category: Stout CD]] |
| - | [[Category: Yamaguchi, M]] | + | [[Category: Yamaguchi M]] |
| - | [[Category: Membrane domain dimer]]
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| - | [[Category: Membrane protein]]
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