1llq
From Proteopedia
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| - | [[Image:1llq.jpg|left|200px]] | + | [[Image:1llq.jpg|left|200px]] |
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| - | '''Crystal Structure of Malic Enzyme from Ascaris suum Complexed with Nicotinamide Adenine Dinucleotide''' | + | {{Structure |
| + | |PDB= 1llq |SIZE=350|CAPTION= <scene name='initialview01'>1llq</scene>, resolution 2.3Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Malate_dehydrogenase_(oxaloacetate-decarboxylating) Malate dehydrogenase (oxaloacetate-decarboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.38 1.1.1.38] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of Malic Enzyme from Ascaris suum Complexed with Nicotinamide Adenine Dinucleotide''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LLQ is a [ | + | 1LLQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLQ OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of the malic enzyme from Ascaris suum complexed with nicotinamide adenine dinucleotide at 2.3 A resolution., Coleman DE, Rao GS, Goldsmith EJ, Cook PF, Harris BG, Biochemistry. 2002 Jun 4;41(22):6928-38. PMID:[http:// | + | Crystal structure of the malic enzyme from Ascaris suum complexed with nicotinamide adenine dinucleotide at 2.3 A resolution., Coleman DE, Rao GS, Goldsmith EJ, Cook PF, Harris BG, Biochemistry. 2002 Jun 4;41(22):6928-38. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12033925 12033925] |
[[Category: Ascaris suum]] | [[Category: Ascaris suum]] | ||
[[Category: Malate dehydrogenase (oxaloacetate-decarboxylating)]] | [[Category: Malate dehydrogenase (oxaloacetate-decarboxylating)]] | ||
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[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:32:22 2008'' |
Revision as of 10:32, 20 March 2008
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| , resolution 2.3Å | |||||||
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| Ligands: | |||||||
| Activity: | Malate dehydrogenase (oxaloacetate-decarboxylating), with EC number 1.1.1.38 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Malic Enzyme from Ascaris suum Complexed with Nicotinamide Adenine Dinucleotide
Overview
The structure of the Ascaris suum mitochondrial NAD-malic enzyme in binary complex with NAD has been solved to a resolution of 2.3 A by X-ray crystallography. The structure resembles that of the human mitochondrial enzyme determined in complex with NAD [Xu, Y., Bhargava, G., Wu, H., Loeber, G., and Tong, L. (1999) Structure 7, 877-889]. The enzyme is a tetramer comprised of subunits possessing four domains organized in an "open" structure typical of the NAD-bound form. The subunit organization, as in the human enzyme, is a dimer of dimers. The Ascaris enzyme contains 30 additional residues at its amino terminus relative to the human enzyme. These residues significantly increase the interactions that promote tetramer formation and give rise to different subunit-subunit interactions. Unlike the mammalian enzyme, the Ascaris malic enzyme is not regulated by ATP, and no ATP binding site is observed in this structure. Although the active sites of the two enzymes are similar, residues interacting with NAD differ between the two. The structure is discussed in terms of the mechanism and particularly with respect to previously obtained kinetic and site-directed mutagenesis experiments.
About this Structure
1LLQ is a Single protein structure of sequence from Ascaris suum. Full crystallographic information is available from OCA.
Reference
Crystal structure of the malic enzyme from Ascaris suum complexed with nicotinamide adenine dinucleotide at 2.3 A resolution., Coleman DE, Rao GS, Goldsmith EJ, Cook PF, Harris BG, Biochemistry. 2002 Jun 4;41(22):6928-38. PMID:12033925
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