4O93

Crystal structure of Thermus thermophilis transhydrogeanse domain II dimer

Summary for 4O93

• Entry DOI: 10.2210/pdb4o93/pdb
• Descriptor: NAD(P) transhydrogenase subunit alpha 2, NAD(P) transhydrogenase subunit beta, MERCURY (II) ION, ... (4 entities in total)
• Functional Keywords: membrane domain dimer, membrane protein
• Biological source: Thermus thermophilus; More
• Total number of polymer chains: 4
• Total formula weight: 76956.78

Authors

Leung, J.H.,Yamaguchi, M.,Moeller, A.,Schurig-Briccio, L.A.,Gennis, R.B.,Potter, C.S.,Carragher, B.,Stout, C.D. (deposition date: 2013-12-31, release date: 2014-12-31, Last modification date: 2024-02-28)

Primary citation

Leung, J.H.,Schurig-Briccio, L.A.,Yamaguchi, M.,Moeller, A.,Speir, J.A.,Gennis, R.B.,Stout, C.D.
Structural biology. Division of labor in transhydrogenase by alternating proton translocation and hydride transfer.
Science, 347:178-181, 2015

PubMed Abstract: 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 Å crystal structure of the transmembrane proton channel domain of TH from Thermus thermophilus and the 6.9 Å 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.

PubMed: 25574024
DOI: 10.1126/science.1260451

Experimental method

X-RAY DIFFRACTION (2.77 Å)