1jlv: Difference between revisions

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[[Image:1jlv.gif|left|200px]]
{{Seed}}
[[Image:1jlv.png|left|200px]]


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{{STRUCTURE_1jlv|  PDB=1jlv  |  SCENE=  }}  
{{STRUCTURE_1jlv|  PDB=1jlv  |  SCENE=  }}  


'''Anopheles dirus species B glutathione S-transferases 1-3'''
===Anopheles dirus species B glutathione S-transferases 1-3===




==Overview==
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Glutathione S-transferases (GSTs) are dimeric proteins that play an important role in cellular detoxification. Four GSTs from the mosquito Anopheles dirus species B (Ad), an important malaria vector in South East Asia, are produced by alternate splicing of a single transcription product and were previously shown to have detoxifying activity towards pesticides such as DDT. We have determined the crystal structures for two of these alternatively spliced proteins, AdGST1-3 (complexed with glutathione) and AdGST1-4 (apo form), at 1.75 and 2.45 A resolution, respectively. These GST isozymes show differences from the related GST from the Australian sheep blowfly Lucilia cuprina; in particular, the presence of a C-terminal helix forming part of the active site. This helix causes the active site of the Anopheles GSTs to be enclosed. The glutathione-binding helix alpha2 and flanking residues are disordered in the AdGST1-4 (apo) structure, yet ordered in the AdGST1-3 (GSH-bound) structure, suggesting that insect GSTs operate with an induced fit mechanism similar to that found in the plant phi- and human pi-class GSTs. Despite the high overall sequence identities, the active site residues of AdGST1-4 and AdGST1-3 have different conformations.
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{{ABSTRACT_PUBMED_11604524}}


==About this Structure==
==About this Structure==
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[[Category: Glutathione s-transferase]]
[[Category: Glutathione s-transferase]]
[[Category: Gst]]
[[Category: Gst]]
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