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| {{STRUCTURE_1jlv| PDB=1jlv | SCENE= }} | | {{STRUCTURE_1jlv| PDB=1jlv | SCENE= }} |
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| '''Anopheles dirus species B glutathione S-transferases 1-3'''
| | ===Anopheles dirus species B glutathione S-transferases 1-3=== |
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| ==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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11604524}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11604524 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11604524}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Glutathione s-transferase]] | | [[Category: Glutathione s-transferase]] |
| [[Category: Gst]] | | [[Category: Gst]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:23:00 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:26:49 2008'' |