4o93: Difference between revisions

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<StructureSection load='4o93' size='340' side='right'caption='[[4o93]], [[Resolution|resolution]] 2.77&Aring;' scene=''>
<StructureSection load='4o93' size='340' side='right'caption='[[4o93]], [[Resolution|resolution]] 2.77&Aring;' 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]] 2.77&#8491;</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;">
== Publication Abstract from PubMed ==
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.
 
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>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4o93" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[NAD(P) transhydrogenase|NAD(P) transhydrogenase]]
*[[NAD(P) transhydrogenase 3D structures|NAD(P) transhydrogenase 3D structures]]
== References ==
<references/>
__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]]
[[Category: Membrane protein]]
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