1okt
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1okt.jpg|left|200px]] | + | [[Image:1okt.jpg|left|200px]] |
| - | + | ||
| - | '''X-RAY STRUCTURE OF GLUTATHIONE S-TRANSFERASE FROM THE MALARIAL PARASITE PLASMODIUM FALCIPARUM''' | + | {{Structure |
| + | |PDB= 1okt |SIZE=350|CAPTION= <scene name='initialview01'>1okt</scene>, resolution 1.90Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Fmt+Binding+Site+For+Chain+B'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=FMT:FORMIC ACID'>FMT</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''X-RAY STRUCTURE OF GLUTATHIONE S-TRANSFERASE FROM THE MALARIAL PARASITE PLASMODIUM FALCIPARUM''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1OKT is a [ | + | 1OKT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKT OCA]. |
==Reference== | ==Reference== | ||
| - | X-ray structure of glutathione S-transferase from the malarial parasite Plasmodium falciparum., Fritz-Wolf K, Becker A, Rahlfs S, Harwaldt P, Schirmer RH, Kabsch W, Becker K, Proc Natl Acad Sci U S A. 2003 Nov 25;100(24):13821-6. Epub 2003 Nov 17. PMID:[http:// | + | X-ray structure of glutathione S-transferase from the malarial parasite Plasmodium falciparum., Fritz-Wolf K, Becker A, Rahlfs S, Harwaldt P, Schirmer RH, Kabsch W, Becker K, Proc Natl Acad Sci U S A. 2003 Nov 25;100(24):13821-6. Epub 2003 Nov 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14623980 14623980] |
[[Category: Glutathione transferase]] | [[Category: Glutathione transferase]] | ||
[[Category: Plasmodium falciparum]] | [[Category: Plasmodium falciparum]] | ||
| Line 26: | Line 35: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''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 13:12:15 2008'' |
Revision as of 11:12, 20 March 2008
| |||||||
| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Glutathione transferase, with EC number 2.5.1.18 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-RAY STRUCTURE OF GLUTATHIONE S-TRANSFERASE FROM THE MALARIAL PARASITE PLASMODIUM FALCIPARUM
Overview
GSTs catalyze the conjugation of glutathione with a wide variety of hydrophobic compounds, generally resulting in nontoxic products that can be readily eliminated. In contrast to many other organisms, the malarial parasite Plasmodium falciparum possesses only one GST isoenzyme (PfGST). This GST is highly abundant in the parasite, its activity was found to be increased in chloroquine-resistant cells, and it has been shown to act as a ligandin for parasitotoxic hemin. Thus, the enzyme represents a promising target for antimalarial drug development. We now have solved the crystal structure of PfGST at a resolution of 1.9 A. The homodimeric protein of 26 kDa per subunit represents a GST form that cannot be assigned to any of the known GST classes. In comparison to other GSTs, and, in particular, to the human isoforms, PfGST possesses a shorter C-terminal section resulting in a more solvent-accessible binding site for the hydrophobic and amphiphilic substrates. The structure furthermore reveals features in this region that could be exploited for the design of specific PfGST inhibitors.
About this Structure
1OKT is a Single protein structure of sequence from Plasmodium falciparum. Full crystallographic information is available from OCA.
Reference
X-ray structure of glutathione S-transferase from the malarial parasite Plasmodium falciparum., Fritz-Wolf K, Becker A, Rahlfs S, Harwaldt P, Schirmer RH, Kabsch W, Becker K, Proc Natl Acad Sci U S A. 2003 Nov 25;100(24):13821-6. Epub 2003 Nov 17. PMID:14623980
Page seeded by OCA on Thu Mar 20 13:12:15 2008
