4o93: Difference between revisions

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 ==Crystal structure of Thermus thermophilis transhydrogeanse domain II dimer==
-<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 ==
-<table><tr><td colspan='2'>[[4o93]] is a 4 chain structure. 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='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='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='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>
+<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>
 </table>
 == 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==
-*[[NAD(P) transhydrogenase|NAD(P) transhydrogenase]]
+*[[NAD(P) transhydrogenase 3D structures|NAD(P) transhydrogenase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Carragher, B]]
+[[Category: Large Structures]]
-[[Category: Gennis, R B]]
+[[Category: Thermus thermophilus HB27]]
-[[Category: Leung, J H]]
+[[Category: Carragher B]]
-[[Category: Moeller, A]]
+[[Category: Gennis RB]]
-[[Category: Potter, C S]]
+[[Category: Leung JH]]
-[[Category: Schurig-Briccio, L A]]
+[[Category: Moeller A]]
-[[Category: Stout, C D]]
+[[Category: Potter CS]]
-[[Category: Yamaguchi, M]]
+[[Category: Schurig-Briccio LA]]
-[[Category: Membrane domain dimer]]
+[[Category: Stout CD]]
-[[Category: Membrane protein]]
+[[Category: Yamaguchi M]]