1tu8
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=GTX:S-HEXYLGLUTATHIONE'>GTX</scene> | |LIGAND= <scene name='pdbligand=GTX:S-HEXYLGLUTATHIONE'>GTX</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] | + | |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> |
|GENE= GST2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6282 Onchocerca volvulus]) | |GENE= GST2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6282 Onchocerca volvulus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1tu7|1TU7]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tu8 OCA], [http://www.ebi.ac.uk/pdbsum/1tu8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tu8 RCSB]</span> | ||
}} | }} | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Perbandt, M.]] | [[Category: Perbandt, M.]] | ||
| - | [[Category: GTX]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:01:07 2008'' |
Revision as of 21:01, 30 March 2008
| |||||||
| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | GST2 (Onchocerca volvulus) | ||||||
| Activity: | Glutathione transferase, with EC number 2.5.1.18 | ||||||
| Related: | 1TU7
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STructure of Onchoverca volvulus Pi-class Glutathione S-transferase with its kompetitive inhibitor s-hexyl-GSH
Overview
Onchocerciasis is a debilitating parasitic disease caused by the filarial worm Onchocerca volvulus. Similar to other helminth parasites, O. volvulus is capable of evading the host's immune responses by a variety of defense mechanisms, including the detoxification activities of the glutathione S-transferases (GSTs). Additionally, in response to drug treatment, helminth GSTs are highly up-regulated, making them tempting targets both for chemotherapy and for vaccine development. We analyzed the three-dimensional x-ray structure of the major cytosolic GST from O. volvulus (Ov-GST2) in complex with its natural substrate glutathione and its competitive inhibitor S-hexylglutathione at 1.5 and 1.8 angstrom resolution, respectively. From the perspective of the biochemical classification, the Ov-GST2 seems to be related to pi-class GSTs. However, in comparison to other pi-class GSTs, in particular to the host's counterpart, the Ov-GST2 reveals significant and unusual differences in the sequence and overall structure. Major differences can be found in helix alpha-2, an important region for substrate recognition. Moreover, the binding site for the electrophilic co-substrate is spatially increased and more solvent-accessible. These structural alterations are responsible for different substrate specificities and will form the basis of parasite-specific structure-based drug design investigations.
About this Structure
1TU8 is a Single protein structure of sequence from Onchocerca volvulus. Full crystallographic information is available from OCA.
Reference
Structure of the major cytosolic glutathione S-transferase from the parasitic nematode Onchocerca volvulus., Perbandt M, Hoppner J, Betzel C, Walter RD, Liebau E, J Biol Chem. 2005 Apr 1;280(13):12630-6. Epub 2005 Jan 7. PMID:15640152
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