4o9t: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 8: | Line 8: | ||
== 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] | [[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__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:51, 28 January 2015
Mechanism of transhydrogenase coupling proton translocation and hydride transfer
| ||||||||||||
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
- Integral membrane component of thermus thermophilus transhydrogenase
- Membrane protein
- Nicotinamide nucleotide transhydrogenase couples the proton motive force to nadph formation
- Periplasmic membrane and cytosol
- Proton translocation and hydride transfer
- Respiratory enzyme