4o9u: Difference between revisions
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''' | ==Mechanism of transhydrogenase coupling proton translocation and hydride transfer== | ||
<StructureSection load='4o9u' size='340' side='right' caption='[[4o9u]], [[Resolution|resolution]] 6.93Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4o9u]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O9U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O9U FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o9u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o9u RCSB], [http://www.ebi.ac.uk/pdbsum/4o9u PDBsum]</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] | |||
<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> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Carragher, B]] | [[Category: Carragher, B]] | ||
[[Category: Gennis, R B]] | |||
[[Category: Leung, J H]] | |||
[[Category: Moeller, A]] | |||
[[Category: Potter, C S]] | |||
[[Category: Schurig-Briccio, L A]] | |||
[[Category: Stout, C D]] | |||
[[Category: Yamaguchi, M]] | [[Category: Yamaguchi, M]] | ||
[[Category: | [[Category: Alpha2]] | ||
[[Category: | [[Category: And domain iii as a dimer]] | ||
[[Category: | [[Category: Couples proton motive]] | ||
[[Category: Holo-transhydrogease from thermus thermophilus assembled from subunits alpha1]] | |||
[[Category: Hydride transfer]] | |||
[[Category: Membrane protein]] | |||
[[Category: Nicotinamide nucleotide transhydrogenase]] | |||
[[Category: Periplasmic membrane and cytosol]] | |||
[[Category: Proton translocation and hydride transfer]] | |||
[[Category: Truncated beta]] | |||
Revision as of 16:40, 28 January 2015
Mechanism of transhydrogenase coupling proton translocation and hydride transfer
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Proteopedia Page Contributors and Editors (what is this?)
Categories:
- Carragher, B
- Gennis, R B
- Leung, J H
- Moeller, A
- Potter, C S
- Schurig-Briccio, L A
- Stout, C D
- Yamaguchi, M
- Alpha2
- And domain iii as a dimer
- Couples proton motive
- Holo-transhydrogease from thermus thermophilus assembled from subunits alpha1
- Hydride transfer
- Membrane protein
- Nicotinamide nucleotide transhydrogenase
- Periplasmic membrane and cytosol
- Proton translocation and hydride transfer
- Truncated beta
