4O93

Crystal structure of Thermus thermophilis transhydrogeanse domain II dimer

4O93 の概要

• エントリーDOI: 10.2210/pdb4o93/pdb
• 分子名称: NAD(P) transhydrogenase subunit alpha 2, NAD(P) transhydrogenase subunit beta, MERCURY (II) ION, ... (4 entities in total)
• 機能のキーワード: membrane domain dimer, membrane protein
• 由来する生物種: Thermus thermophilus; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 76956.78

構造登録者

Leung, J.H.,Yamaguchi, M.,Moeller, A.,Schurig-Briccio, L.A.,Gennis, R.B.,Potter, C.S.,Carragher, B.,Stout, C.D. (登録日: 2013-12-31, 公開日: 2014-12-31, 最終更新日: 2024-02-28)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.77 Å)