1tu8

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1tu8, resolution 1.80Å ()
Ligands:
Gene: GST2 (Onchocerca volvulus)
Activity: Glutathione transferase, with EC number 2.5.1.18
Related: 1tu7
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Contents

STructure of Onchoverca volvulus Pi-class Glutathione S-transferase with its kompetitive inhibitor s-hexyl-GSH

Publication Abstract from PubMed

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1tu8 is a 4 chain structure with sequence from Onchocerca volvulus. Full crystallographic information is available from OCA.

See Also

Reference

  • Perbandt M, Hoppner J, Betzel C, Walter RD, Liebau E. Structure of the major cytosolic glutathione S-transferase from the parasitic nematode Onchocerca volvulus. J Biol Chem. 2005 Apr 1;280(13):12630-6. Epub 2005 Jan 7. PMID:15640152 doi:http://dx.doi.org/10.1074/jbc.M413551200

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