1llq: Difference between revisions
New page: left|200px<br /><applet load="1llq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1llq, resolution 2.3Å" /> '''Crystal Structure of ... |
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[[Image:1llq.jpg|left|200px]]<br /><applet load="1llq" size=" | [[Image:1llq.jpg|left|200px]]<br /><applet load="1llq" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1llq, resolution 2.3Å" /> | caption="1llq, resolution 2.3Å" /> | ||
'''Crystal Structure of Malic Enzyme from Ascaris suum Complexed with Nicotinamide Adenine Dinucleotide'''<br /> | '''Crystal Structure of Malic Enzyme from Ascaris suum Complexed with Nicotinamide Adenine Dinucleotide'''<br /> | ||
==Overview== | ==Overview== | ||
The structure of the Ascaris suum mitochondrial NAD-malic enzyme in binary | 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== | ==About this Structure== | ||
1LLQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum] with NAD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | 1LLQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum] with <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLQ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Malate dehydrogenase (oxaloacetate-decarboxylating)]] | [[Category: Malate dehydrogenase (oxaloacetate-decarboxylating)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Coleman, D | [[Category: Coleman, D E.]] | ||
[[Category: Cook, P | [[Category: Cook, P F.]] | ||
[[Category: Goldsmith, E | [[Category: Goldsmith, E J.]] | ||
[[Category: Harris, B | [[Category: Harris, B G.]] | ||
[[Category: Jagannatha, G | [[Category: Jagannatha, G S.]] | ||
[[Category: NAD]] | [[Category: NAD]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:08 2008'' | ||
Revision as of 14:46, 21 February 2008
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Crystal Structure of Malic Enzyme from Ascaris suum Complexed with Nicotinamide Adenine Dinucleotide
OverviewOverview
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 StructureAbout this Structure
1LLQ is a Single protein structure of sequence from Ascaris suum with as ligand. Active as Malate dehydrogenase (oxaloacetate-decarboxylating), with EC number 1.1.1.38 Full crystallographic information is available from OCA.
ReferenceReference
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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