1HZZ

THE ASYMMETRIC COMPLEX OF THE TWO NUCLEOTIDE-BINDING COMPONENTS (DI, DIII) OF PROTON-TRANSLOCATING TRANSHYDROGENASE

Summary for 1HZZ

• Entry DOI: 10.2210/pdb1hzz/pdb
• Related: 1DJL 1E3T 1F8G
• Descriptor: PROTON-TRANSLOCATING NICOTINAMIDE NUCLEOTIDE TRANSHYDROGENASE SUBUNIT PNTAA, PROTON-TRANSLOCATING NICOTINAMIDE NUCLEOTIDE TRANSHYDROGENASE SUBUNIT PNTB, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (5 entities in total)
• Functional Keywords: rossmann fold, alpha beta repeat, nucleotide-binding fold, oxidoreductase
• Biological source: Rhodospirillum rubrum; More
• Cellular location: Cell inner membrane; Multi-pass membrane protein (By similarity): Q59765
• Total number of polymer chains: 3
• Total formula weight: 103541.91

Authors

Cotton, N.P.J.,White, S.A.,Peake, S.J.,McSweeney, S.,Jackson, J.B. (deposition date: 2001-01-27, release date: 2001-08-29, Last modification date: 2024-02-07)

Primary citation

Cotton, N.P.,White, S.A.,Peake, S.J.,McSweeney, S.,Jackson, J.B.
The crystal structure of an asymmetric complex of the two nucleotide binding components of proton-translocating transhydrogenase.
Structure, 9:165-176, 2001

PubMed Abstract: Membrane-bound ion translocators have important functions in biology, but their mechanisms of action are often poorly understood. Transhydrogenase, found in animal mitochondria and bacteria, links the redox reaction between NAD(H) and NADP(H) to proton translocation across a membrane. Linkage is achieved through changes in protein conformation at the nucleotide binding sites. The redox reaction takes place between two protein components located on the membrane surface: dI, which binds NAD(H), and dIII, which binds NADP(H). A third component, dII, provides a proton channel through the membrane. Intact membrane-located transhydrogenase is probably a dimer (two copies each of dI, dII, and dIII).

PubMed: 11250201
DOI: 10.1016/S0969-2126(01)00571-8

Experimental method

X-RAY DIFFRACTION (2.5 Å)