1do8
From Proteopedia
(New page: 200px<br /> <applet load="1do8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1do8, resolution 2.2Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1do8.gif|left|200px]]<br /> | + | [[Image:1do8.gif|left|200px]]<br /><applet load="1do8" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1do8" size=" | + | |
caption="1do8, resolution 2.2Å" /> | caption="1do8, resolution 2.2Å" /> | ||
'''CRYSTAL STRUCTURE OF A CLOSED FORM OF HUMAN MITOCHONDRIAL NAD(P)+-DEPENDENT MALIC ENZYME'''<br /> | '''CRYSTAL STRUCTURE OF A CLOSED FORM OF HUMAN MITOCHONDRIAL NAD(P)+-DEPENDENT MALIC ENZYME'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Malic enzymes are widely distributed in nature and have many biological | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DO8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with OXL, MN and NAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1DO8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=OXL:'>OXL</scene>, <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DO8 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Malate dehydrogenase (decarboxylating)]] | [[Category: Malate dehydrogenase (decarboxylating)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Floyd, D | + | [[Category: Floyd, D L.]] |
[[Category: Loeber, G.]] | [[Category: Loeber, G.]] | ||
[[Category: Tong, L.]] | [[Category: Tong, L.]] | ||
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[[Category: oxidative decarboxylase]] | [[Category: oxidative decarboxylase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:41 2008'' |
Revision as of 10:18, 21 February 2008
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CRYSTAL STRUCTURE OF A CLOSED FORM OF HUMAN MITOCHONDRIAL NAD(P)+-DEPENDENT MALIC ENZYME
Contents |
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
1DO8 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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