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4o9p
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Thermus thermophilis transhydrogeanse domain II dimer SeMet derivative== | |
| + | <StructureSection load='4o9p' size='340' side='right'caption='[[4o9p]], [[Resolution|resolution]] 2.89Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4o9p]] 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=4O9P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O9P FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4o9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o9p OCA], [https://pdbe.org/4o9p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o9p RCSB], [https://www.ebi.ac.uk/pdbsum/4o9p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o9p ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4o9p" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[NAD(P) transhydrogenase 3D structures|NAD(P) transhydrogenase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermus thermophilus HB27]] | ||
| + | [[Category: Carragher B]] | ||
| + | [[Category: Gennis RB]] | ||
| + | [[Category: Leung JH]] | ||
| + | [[Category: Moeller A]] | ||
| + | [[Category: Potter CS]] | ||
| + | [[Category: Schurig-Briccio LA]] | ||
| + | [[Category: Stout CD]] | ||
| + | [[Category: Yamaguchi M]] | ||
Current revision
Crystal structure of Thermus thermophilis transhydrogeanse domain II dimer SeMet derivative
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