1qr6: Difference between revisions

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[[Image:1qr6.jpg|left|200px]]<br /><applet load="1qr6" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1qr6.jpg|left|200px]]
caption="1qr6, resolution 2.1&Aring;" />
 
'''HUMAN MITOCHONDRIAL NAD(P)-DEPENDENT MALIC ENZYME'''<br />
{{Structure
|PDB= 1qr6 |SIZE=350|CAPTION= <scene name='initialview01'>1qr6</scene>, resolution 2.1&Aring;
|SITE=
|LIGAND= <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]
|GENE=
}}
 
'''HUMAN MITOCHONDRIAL NAD(P)-DEPENDENT MALIC ENZYME'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1QR6 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=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1QR6 OCA].  
1QR6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QR6 OCA].  


==Reference==
==Reference==
Crystal structure of human mitochondrial NAD(P)(+)-dependent malic enzyme: a new class of oxidative decarboxylases., Xu Y, Bhargava G, Wu H, Loeber G, Tong L, Structure. 1999;7(8):877-889. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10467136 10467136]
Crystal structure of human mitochondrial NAD(P)(+)-dependent malic enzyme: a new class of oxidative decarboxylases., Xu Y, Bhargava G, Wu H, Loeber G, Tong L, Structure. 1999;7(8):877-889. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10467136 10467136]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Malate dehydrogenase (decarboxylating)]]
[[Category: Malate dehydrogenase (decarboxylating)]]
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[[Category: Xu, Y.]]
[[Category: Xu, Y.]]
[[Category: NAD]]
[[Category: NAD]]
[[Category: four domains]]
[[Category: four domain]]
[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
[[Category: rossmann fold]]
[[Category: rossmann fold]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:42:54 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:41:33 2008''

Revision as of 14:41, 20 March 2008

File:1qr6.jpg


PDB ID 1qr6

Drag the structure with the mouse to rotate
, resolution 2.1Å
Ligands:
Activity: Malate dehydrogenase (decarboxylating), with EC number 1.1.1.39
Coordinates: save as pdb, mmCIF, xml



HUMAN MITOCHONDRIAL NAD(P)-DEPENDENT MALIC ENZYME


OverviewOverview

Background: Malic enzymes catalyze the oxidative decarboxylation of malate to pyruvate and CO(2) with the concomitant reduction of NAD(P)(+) to NAD(P)H. They are widely distributed in nature and have important biological functions. Human mitochondrial NAD(P)(+)-dependent malic enzyme (mNAD-ME) may have a crucial role in the metabolism of glutamine for energy production in rapidly dividing cells and tumors. Moreover, this isoform is unique among malic enzymes in that it is a cooperative enzyme, and its activity is controlled allosterically. Results: The crystal structure of human mNAD-ME has been determined at 2.5 A resolution by the selenomethionyl multiwavelength anomalous diffraction method and refined to 2.1 A resolution. The structure of the monomer can be divided into four domains; the active site of the enzyme is located in a deep cleft at the interface between three of the domains. Three acidic residues (Glu255, Asp256 and Asp279) were identified as ligands for the divalent cation that is required for catalysis by malic enzymes. Conclusions: The structure reveals that malic enzymes belong to a new class of oxidative decarboxylases. The tetramer of the enzyme appears to be a dimer of dimers. The active site of each monomer is located far from the tetramer interface. The structure also shows the binding of a second NAD(+) molecule in a pocket 35 A away from the active site. The natural ligand for this second binding site may be ATP, an allosteric inhibitor of the enzyme.

DiseaseDisease

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

About this StructureAbout this Structure

1QR6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of human mitochondrial NAD(P)(+)-dependent malic enzyme: a new class of oxidative decarboxylases., Xu Y, Bhargava G, Wu H, Loeber G, Tong L, Structure. 1999;7(8):877-889. PMID:10467136

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