1llq: Difference between revisions

Revision as of 21:23, 2 July 2008

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File:1llq.png

Template:STRUCTURE 1llq

Crystal Structure of Malic Enzyme from Ascaris suum Complexed with Nicotinamide Adenine DinucleotideCrystal Structure of Malic Enzyme from Ascaris suum Complexed with Nicotinamide Adenine Dinucleotide

Template:ABSTRACT PUBMED 12033925

About this StructureAbout this Structure

1LLQ is a Single protein structure of sequence from Ascaris suum. 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure of Malic Enzyme from Ascaris suum Complexed with Nicotinamide Adenine Dinucleotide'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12033925}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12033925 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12033925}}
 ==About this Structure==
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 [[Category: Oxidoreductase]]
 [[Category: Rossmann fold]]
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