1D4O

CRYSTAL STRUCTURE OF TRANSHYDROGENASE DOMAIN III AT 1.2 ANGSTROMS RESOLUTION

1D4O の概要

• エントリーDOI: 10.2210/pdb1d4o/pdb
• 分子名称: NADP(H) TRANSHYDROGENASE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: nucleotide-binding fold, protein-nadp(h) complex, inverted binding of nadp(h), oxidoreductase
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Mitochondrion inner membrane ; Multi-pass membrane protein ; Matrix side : P11024
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20761.47

構造登録者

Prasad, G.S.,Sridhar, V.,Yamaguchi, M.,Hatefi, Y.,Stout, C.D. (登録日: 1999-10-04, 公開日: 2000-01-20, 最終更新日: 2024-02-07)

主引用文献

Prasad, G.S.,Sridhar, V.,Yamaguchi, M.,Hatefi, Y.,Stout, C.D.
Crystal structure of transhydrogenase domain III at 1.2 A resolution.
Nat.Struct.Biol., 6:1126-1131, 1999

PubMed Abstract: The nicotinamide nucleotide transhydrogenases (TH) of mitochondria and bacteria are membrane-intercalated proton pumps that transduce substrate binding energy and protonmotive force via protein conformational changes. In mitochondria, TH utilizes protonmotive force to promote direct hydride ion transfer from NADH to NADP, which are bound at the distinct extramembranous domains I and III, respectively. Domain II is the membrane-intercalated domain and contains the enzyme's proton channel. This paper describes the crystal structure of the NADP(H) binding domain III of bovine TH at 1.2 A resolution. The structure reveals that NADP is bound in a manner inverted from that previously observed for nucleotide binding folds. The non-classical binding mode exposes the NADP(H) nicotinamide ring for direct contact with NAD(H) in domain I, in accord with biochemical data. The surface of domain III surrounding the exposed nicotinamide is comprised of conserved residues presumed to form the interface with domain I during hydride ion transfer. Further, an adjacent region contains a number of acidic residues, forming a surface with negative electrostatic potential which may interact with extramembranous loops of domain II. Together, the distinctive surface features allow mechanistic considerations regarding the NADP(H)-promoted conformation changes that are involved in the interactions of domain III with domains I and II for hydride ion transfer and proton translocation.

PubMed: 10581554
DOI: 10.1038/70067

実験手法

X-RAY DIFFRACTION (1.21 Å)