9v69

X-ray crystal structure of the two-electron reduced form of wild type b5R

spinqualitylabelsall models 9v69, resolution 0.96Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9v69 is a 1 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 0.96Å Ligands: FDA, NAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NB5R3_PIG Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.[:] Publication Abstract from PubMed Many structural studies have been reported for ferredoxin:NADP(+) reductase family members, but an experimental validation of the catalytic hydride and proton transfer steps through a direct detection of the involved hydrogen atoms has not been achieved so far. Here, we determined high-resolution X-ray and neutron crystal structures of NADH-cytochrome b(5) reductase, which acts as an electron supplier for various metabolic processes and mediates hydride and proton transfer reactions via its FAD and NADH cofactors. The X-ray structures identify the FADH(-)-NAD(+) and FAD-NADH complexes based on the electron densities of the hydrogen atoms bound to the cofactors. The neutron structures determined at different pD-values show a difference in the protonation state of the histidine residue in the hydrogen-bond network from FAD to the protein surface. The observation of the hydrogen atoms reveals the structural basis for the hydride and proton transfer reactions catalyzed by NADH-cytochrome b(5) reductase. Structural basis of hydride and proton transfer reactions revealed by the detection of hydrogen atoms in mammalian NADH-cytochrome b(5) reductase.,Hirano Y, Kurihara K, Kusaka K, Ostermann A, Hikita M, Kimura S, Miki K, Tamada T Structure. 2025 Oct 30:S0969-2126(25)00393-4. doi: 10.1016/j.str.2025.10.006. PMID:41172987 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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