1PJL

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

Summary for 1PJL

• Entry DOI: 10.2210/pdb1pjl/pdb
• Related: 1DO8 1QR6
• Descriptor: NAD-dependent malic enzyme, mitochondrial, LUTETIUM (III) ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion matrix: P23368
• Total number of polymer chains: 8
• Total formula weight: 541813.54

Authors

Yang, Z.,Batra, R.,Floyd, D.L.,Hung, H.-C.,Chang, G.-G.,Tong, L. (deposition date: 2003-06-03, release date: 2003-06-17, Last modification date: 2024-10-30)

Primary citation

Yang, Z.,Batra, R.,Floyd, D.L.,Hung, H.-C.,Chang, G.-G.,Tong, L.
Potent and competitive inhibition of malic enzymes by lanthanide ions
Biochem.Biophys.Res.Commun., 274:440-444, 2000

PubMed Abstract: 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.

PubMed: 10913357
DOI: 10.1006/bbrc.2000.3163

Experimental method

X-RAY DIFFRACTION (2.9 Å)