Literature summary for 7.1.1.1 extracted from

Kampjut, D.; Sazanov, L.A.
Structure and mechanism of mitochondrial proton-translocating transhydrogenase (2019), Nature, 573, 291-295 .

Search for more literature for 7.1.1.1

Cloned(Commentary)

Cloned (Comment)	Organism
-	Ovis aries

Crystallization (Commentary)

Crystallization (Comment)	Organism
cryo-electron microscopy structure in different conformational states. The NADP(H)-binding domain opens the proton channel to the opposite sides of the membrane	Ovis aries

Organism

Organism	UniProt	Comment	Textmining
Ovis aries	W5PFI3	-	-

Synonyms

Synonyms	Comment	Organism
nicotinamide nucleotide transhydrogenase	-	Ovis aries
proton-translocating transhydrogenase	-	Ovis aries

General Information

General Information	Comment	Organism
metabolism	proton translocation and nucleotide exchange are tightly coupled by direct interactions between residue H664 and NADP(H), the attachment and detachment of NADP(H)-bound domain dIII is strictly dependent on the protonation state of H664 and opens the proton channel to the opposite sides of the membrane. The forward reaction occurs under a high proton motive force and an excess of NADP+. After hydride transfer, dIII-NADPH swivels down and attaches to dII-H664, opening it to the P side. This enables the protonation of H664 from the P side. Nucleotide exchange then follows. dIII-NADP+ detaches from dII-H664+, this opens dII to the N side where H664+ is deprotonated. Domain dIII-NADP+ then associates with dI, allowing for hydride transfer. All the steps can be easily reversed in the appropriate conditions	Ovis aries

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Release 2023.1 (January 2023)