1tu7 | pdb_00001tu7

Structure of Onchocerca Volvulus Pi-class Glutathione S-transferase

spinqualitylabelsall models 1tu7, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1tu7 is a 2 chain structure with sequence from Oncvo. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, GSH Related: 1tu8 Gene: GST2 (ONCVO) Activity: Glutathione transferase, with EC number 2.5.1.18 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [GSTP_ONCVO] Appears to play a central role in the parasite detoxification system. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. 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. See Also Glutathione S-transferase

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