4o9t: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4o9t]] is a 8 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=4O9T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O9T FirstGlance]. <br>
<table><tr><td colspan='2'>[[4o9t]] is a 8 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=4O9T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O9T FirstGlance]. <br>
</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=4o9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o9t OCA], [https://pdbe.org/4o9t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o9t RCSB], [https://www.ebi.ac.uk/pdbsum/4o9t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o9t ProSAT]</span></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]] 3.079&#8491;</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=4o9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o9t OCA], [https://pdbe.org/4o9t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o9t RCSB], [https://www.ebi.ac.uk/pdbsum/4o9t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o9t ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/Q72GR9_THET2 Q72GR9_THET2]  
[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 4o9t" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[NAD(P) transhydrogenase 3D structures|NAD(P) transhydrogenase 3D structures]]
*[[NAD(P) transhydrogenase 3D structures|NAD(P) transhydrogenase 3D structures]]
== References ==
<references/>
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</StructureSection>
</StructureSection>

Latest revision as of 12:38, 1 March 2024

Mechanism of transhydrogenase coupling proton translocation and hydride transfer

4o9t, resolution 3.08Å

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