1DJL

THE CRYSTAL STRUCTURE OF HUMAN TRANSHYDROGENASE DOMAIN III WITH BOUND NADP

Summary for 1DJL

• Entry DOI: 10.2210/pdb1djl/pdb
• Descriptor: TRANSHYDROGENASE DIII, SULFATE ION, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (5 entities in total)
• Functional Keywords: rossmann fold dinucleotide binding fold reverse binding of nadp, oxidoreductase
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion inner membrane; Multi-pass membrane protein; Matrix side (Potential): Q13423
• Total number of polymer chains: 2
• Total formula weight: 46426.43

Authors

White, S.A.,Peak, S.J.,Cotton, N.P.,Jackson, J.B. (deposition date: 1999-12-03, release date: 2000-12-06, Last modification date: 2024-02-07)

Primary citation

White, S.A.,Peake, S.J.,McSweeney, S.,Leonard, G.,Cotton, N.P.,Jackson, J.B.
The high-resolution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from human heart mitochondria.
Structure Fold.Des., 8:1-12, 2000

PubMed Abstract: Transhydrogenase, located in the inner membranes of animal mitochondria and the cytoplasmic membranes of bacteria, couples the transfer of reducing equivalents between NAD(H) and NADP(H) to proton pumping. The protein comprises three subunits termed dI, dII and dIII. The dII component spans the membrane. The dI component, which contains the binding site for NAD(+)/NADH, and the dIII component, which has the binding site for NADP(+)/NADPH, protrude from the membrane. Proton pumping is probably coupled to changes in the binding affinities of dIII for NADP(+) and NADPH.

PubMed: 10673423
DOI: 10.1016/S0969-2126(00)00075-7

Experimental method

X-RAY DIFFRACTION (2 Å)