1jlw
From Proteopedia
(New page: 200px<br /><applet load="1jlw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jlw, resolution 2.45Å" /> '''Anopheles dirus spec...) |
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| - | [[Image:1jlw.gif|left|200px]]<br /><applet load="1jlw" size=" | + | [[Image:1jlw.gif|left|200px]]<br /><applet load="1jlw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jlw, resolution 2.45Å" /> | caption="1jlw, resolution 2.45Å" /> | ||
'''Anopheles dirus species B glutathione S-transferases 1-4'''<br /> | '''Anopheles dirus species B glutathione S-transferases 1-4'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Glutathione S-transferases (GSTs) are dimeric proteins that play an | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1JLW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anopheles_cracens Anopheles cracens]. Active as [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] Full crystallographic information is available from [http:// | + | 1JLW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anopheles_cracens Anopheles cracens]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JLW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Harnnoi, T.]] | [[Category: Harnnoi, T.]] | ||
[[Category: Jirajaroenrat, K.]] | [[Category: Jirajaroenrat, K.]] | ||
| - | [[Category: Ketterman, A | + | [[Category: Ketterman, A J.]] |
| - | [[Category: Oakley, A | + | [[Category: Oakley, A J.]] |
[[Category: Udomsinprasert, R.]] | [[Category: Udomsinprasert, R.]] | ||
| - | [[Category: Wilce, M | + | [[Category: Wilce, M C.]] |
[[Category: adgst1-4]] | [[Category: adgst1-4]] | ||
[[Category: glutathione s-transferase]] | [[Category: glutathione s-transferase]] | ||
[[Category: gst]] | [[Category: gst]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:24:08 2008'' |
Revision as of 11:24, 21 February 2008
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Anopheles dirus species B glutathione S-transferases 1-4
Overview
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.
About this Structure
1JLW is a Single protein structure of sequence from Anopheles cracens. Active as Glutathione transferase, with EC number 2.5.1.18 Full crystallographic information is available from OCA.
Reference
The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B., Oakley AJ, Harnnoi T, Udomsinprasert R, Jirajaroenrat K, Ketterman AJ, Wilce MC, Protein Sci. 2001 Nov;10(11):2176-85. PMID:11604524
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