1efl

From Proteopedia

Revision as of 13:42, 15 February 2008

HUMAN MALIC ENZYME IN A QUATERNARY COMPLEX WITH NAD, MG, AND TARTRONATE

Overview

Malic enzymes are widely distributed in nature and have many biological, functions. The crystal structure of human mitochondrial NAD(P)+-dependent, malic enzyme in a quaternary complex with NAD+, Mn++ and oxalate has been, determined at 2.2 A resolution. The structures of the quaternary complex, with NAD+, Mg++, tartronate or ketomalonate have been determined at 2.6 A, resolution. The structures show the enzyme in a closed form in these, complexes and reveal the binding modes of the cation and the inhibitors., The divalent cation is coordinated in an octahedral fashion by six, ligating oxygens, two from the substrate/inhibitor, three from Glu 255, Asp 256 and Asp 279 of the enzyme, and one from a water molecule. The, structural information has significant implications for the catalytic, mechanism of malic enzymes and identifies Tyr 112 and Lys 183 as possible, catalytic residues. Changes in tetramer organization of the enzyme are, also observed in these complexes, which might be relevant for its, cooperative behavior and allosteric control.

Disease

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

About this Structure

1EFL is a Single protein structure of sequence from Homo sapiens with , and as ligands. Active as Malate dehydrogenase (decarboxylating), with EC number 1.1.1.39 Full crystallographic information is available from OCA.

Reference

Structure of a closed form of human malic enzyme and implications for catalytic mechanism., Yang Z, Floyd DL, Loeber G, Tong L, Nat Struct Biol. 2000 Mar;7(3):251-7. PMID:10700286

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