1pjl

Crystal structure of human m-NAD-ME in ternary complex with NAD and Lu3+

spinqualitylabelsall models 1pjl, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1pjl is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: LU, MSE, NAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MAOM_HUMAN Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The catalytic activity of malic enzyme (ME), a member of a new class of oxidative decarboxylases, requires the presence of divalent cations (Mn(2+), Mg(2+), and others). The crystal structure at 2.9 A resolution of human mitochondrial NAD(+)-dependent malic enzyme in a ternary complex with NAD(+) and the lanthanide ion Lu(3+), which has similar radius as Mn(2+), reveals a new conformation of the enzyme. The active site in this ternary complex is in an open form, while the organization of the tetramer of the enzyme actually resembles that with a closed active site. The Lu(3+) ion is bound to the enzyme at the same site as Mn(2+). Kinetic studies showed that Lu(3+) is a potent inhibitor of both the human NAD(P)(+)-dependent ME and the NADP(+)-dependent ME from pigeon liver, and is competitive with respect to the divalent cation, consistent with the structural information. Potent and competitive inhibition of malic enzymes by lanthanide ions.,Yang Z, Batra R, Floyd DL, Hung HC, Chang GG, Tong L Biochem Biophys Res Commun. 2000 Aug 2;274(2):440-4. PMID:10913357 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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