1okt

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[[Image:1okt.jpg|left|200px]]
[[Image:1okt.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1okt |SIZE=350|CAPTION= <scene name='initialview01'>1okt</scene>, resolution 1.90&Aring;
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The line below this paragraph, containing "STRUCTURE_1okt", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Fmt+Binding+Site+For+Chain+B'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1okt| PDB=1okt | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1okt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1okt OCA], [http://www.ebi.ac.uk/pdbsum/1okt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1okt RCSB]</span>
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}}
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'''X-RAY STRUCTURE OF GLUTATHIONE S-TRANSFERASE FROM THE MALARIAL PARASITE PLASMODIUM FALCIPARUM'''
'''X-RAY STRUCTURE OF GLUTATHIONE S-TRANSFERASE FROM THE MALARIAL PARASITE PLASMODIUM FALCIPARUM'''
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[[Category: Rahlfs, S.]]
[[Category: Rahlfs, S.]]
[[Category: Schirmer, R H.]]
[[Category: Schirmer, R H.]]
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[[Category: gst]]
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[[Category: Gst]]
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[[Category: plasmodium falciparum]]
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[[Category: Plasmodium falciparum]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:58:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:46:45 2008''
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Revision as of 00:58, 3 May 2008

Template:STRUCTURE 1okt

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 Sat May 3 03:58:41 2008

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