1efk
From Proteopedia
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|PDB= 1efk |SIZE=350|CAPTION= <scene name='initialview01'>1efk</scene>, resolution 2.6Å | |PDB= 1efk |SIZE=350|CAPTION= <scene name='initialview01'>1efk</scene>, resolution 2.6Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=MAK:ALPHA-KETOMALONIC+ACID'>MAK</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Malate_dehydrogenase_(decarboxylating) Malate dehydrogenase (decarboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.39 1.1.1.39] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Malate_dehydrogenase_(decarboxylating) Malate dehydrogenase (decarboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.39 1.1.1.39] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1do8|1DO8]], [[1qr6|1QR6]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1efk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1efk OCA], [http://www.ebi.ac.uk/pdbsum/1efk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1efk RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=154270 154270]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Tong, L.]] | [[Category: Tong, L.]] | ||
[[Category: Yang, Z.]] | [[Category: Yang, Z.]] | ||
| - | [[Category: MAK]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: NAD]] | ||
[[Category: closed form]] | [[Category: closed form]] | ||
[[Category: malic enzyme]] | [[Category: malic enzyme]] | ||
[[Category: quaternary complex]] | [[Category: quaternary complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:01:29 2008'' |
Revision as of 17:01, 30 March 2008
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| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | Malate dehydrogenase (decarboxylating), with EC number 1.1.1.39 | ||||||
| Related: | 1DO8, 1QR6
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF HUMAN MALIC ENZYME IN COMPLEX WITH KETOMALONATE
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.
About this Structure
1EFK is a Single protein structure of sequence from Homo sapiens. 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
Page seeded by OCA on Sun Mar 30 20:01:29 2008
