1ywg
From Proteopedia
(New page: 200px<br /><applet load="1ywg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ywg, resolution 2.60Å" /> '''The structure of gly...) |
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| - | [[Image:1ywg.gif|left|200px]]<br /><applet load="1ywg" size=" | + | [[Image:1ywg.gif|left|200px]]<br /><applet load="1ywg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ywg, resolution 2.60Å" /> | caption="1ywg, resolution 2.60Å" /> | ||
'''The structure of glyceraldehyde-3-phosphate dehydrogenase from Plasmodium falciparum'''<br /> | '''The structure of glyceraldehyde-3-phosphate dehydrogenase from Plasmodium falciparum'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The malaria parasite Plasmodium falciparum is responsible for about two | + | The malaria parasite Plasmodium falciparum is responsible for about two million deaths annually, making it important to obtain information about enzymes from this organism that represent potential drug targets. The gene for P. falciparum glyceraldehyde-3-phosphate dehydrogenase (PfGAPDH) has been cloned and the protein expressed as a hexahistidine-tagged recombinant protein in Escherichia coli. The recombinant protein has been crystallized and its three-dimensional structure determined. One molecule of the cofactor NAD+ is bound to each of the four subunits in the tetrameric enzyme. The major structural feature distinguishing human GAPDH from PfGAPDH is the insertion of a dipeptide (-KG-) in the so-called S loop. This insert, together with other characteristic single-amino-acid substitutions, alters the chemical environment of the groove that encompasses the R dyad and that links adjacent cofactor-binding sites and may be responsible for the selective inhibition of the enzyme by ferriprotoporphyrin IX. |
==About this Structure== | ==About this Structure== | ||
| - | 1YWG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum] with NAD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.12 1.2.1.12] Full crystallographic information is available from [http:// | + | 1YWG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum] with <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.12 1.2.1.12] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YWG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Adisa, A.]] | [[Category: Adisa, A.]] | ||
| - | [[Category: Alpyurek, A | + | [[Category: Alpyurek, A E.]] |
| - | [[Category: Colman, P | + | [[Category: Colman, P M.]] |
[[Category: Klonis, N.]] | [[Category: Klonis, N.]] | ||
| - | [[Category: Malby, R | + | [[Category: Malby, R L.]] |
| - | [[Category: Satchell, J | + | [[Category: Satchell, J F.]] |
[[Category: Tilley, L.]] | [[Category: Tilley, L.]] | ||
[[Category: NAD]] | [[Category: NAD]] | ||
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[[Category: tetrameric]] | [[Category: tetrameric]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:09:47 2008'' |
Revision as of 14:09, 21 February 2008
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The structure of glyceraldehyde-3-phosphate dehydrogenase from Plasmodium falciparum
Overview
The malaria parasite Plasmodium falciparum is responsible for about two million deaths annually, making it important to obtain information about enzymes from this organism that represent potential drug targets. The gene for P. falciparum glyceraldehyde-3-phosphate dehydrogenase (PfGAPDH) has been cloned and the protein expressed as a hexahistidine-tagged recombinant protein in Escherichia coli. The recombinant protein has been crystallized and its three-dimensional structure determined. One molecule of the cofactor NAD+ is bound to each of the four subunits in the tetrameric enzyme. The major structural feature distinguishing human GAPDH from PfGAPDH is the insertion of a dipeptide (-KG-) in the so-called S loop. This insert, together with other characteristic single-amino-acid substitutions, alters the chemical environment of the groove that encompasses the R dyad and that links adjacent cofactor-binding sites and may be responsible for the selective inhibition of the enzyme by ferriprotoporphyrin IX.
About this Structure
1YWG is a Single protein structure of sequence from Plasmodium falciparum with as ligand. Active as Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), with EC number 1.2.1.12 Full crystallographic information is available from OCA.
Reference
Structure of glyceraldehyde-3-phosphate dehydrogenase from Plasmodium falciparum., Satchell JF, Malby RL, Luo CS, Adisa A, Alpyurek AE, Klonis N, Smith BJ, Tilley L, Colman PM, Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1213-21. Epub 2005, Aug 16. PMID:16131754
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