1gz3

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Image:1gz3.jpg

1gz3, resolution 2.3Å

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MOLECULAR MECHANISM FOR THE REGULATION OF HUMAN MITOCHONDRIAL NAD(P)+-DEPENDENT MALIC ENZYME BY ATP AND FUMARATE

Contents

Overview

The regulation of human mitochondrial NAD(P)+-dependent malic enzyme, (m-NAD-ME) by ATP and fumarate may be crucial for the metabolism of, glutamine for energy production in rapidly proliferating tissues and, tumors. Here we report the crystal structure at 2.2 A resolution of, m-NAD-ME in complex with ATP, Mn2+, tartronate, and fumarate. Our, structural, kinetic, and mutagenesis studies reveal unexpectedly that ATP, is an active-site inhibitor of the enzyme, despite the presence of an exo, binding site. The structure also reveals the allosteric binding site for, fumarate in the dimer interface. Mutations in this binding site abolished, the activating effects of fumarate. Comparison to the structure in the, absence of fumarate indicates a possible molecular mechanism for the, allosteric function of this compound.

Disease

Known disease associated with this structure: Epilepsy, idopathic generalized, susceptibility to OMIM:[154270]

About this Structure

1GZ3 is a Single protein structure of sequence from Homo sapiens with , , and as ligands. Active as Malate dehydrogenase (oxaloacetate-decarboxylating), with EC number 1.1.1.38 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Molecular mechanism for the regulation of human mitochondrial NAD(P)+-dependent malic enzyme by ATP and fumarate., Yang Z, Lanks CW, Tong L, Structure. 2002 Jul;10(7):951-60. PMID:12121650

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