1jlv
From Proteopedia
(New page: 200px<br /><applet load="1jlv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jlv, resolution 1.75Å" /> '''Anopheles dirus spec...) |
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| - | [[Image:1jlv.gif|left|200px]]<br /><applet load="1jlv" size=" | + | [[Image:1jlv.gif|left|200px]]<br /><applet load="1jlv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jlv, resolution 1.75Å" /> | caption="1jlv, resolution 1.75Å" /> | ||
'''Anopheles dirus species B glutathione S-transferases 1-3'''<br /> | '''Anopheles dirus species B glutathione S-transferases 1-3'''<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== | ||
| - | 1JLV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anopheles_cracens Anopheles cracens] with GSH as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1JLV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anopheles_cracens Anopheles cracens] with <scene name='pdbligand=GSH:'>GSH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1JLV 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: GSH]] | [[Category: GSH]] | ||
[[Category: adgst1-3]] | [[Category: adgst1-3]] | ||
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[[Category: gst]] | [[Category: gst]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:24:12 2008'' |
Revision as of 11:24, 21 February 2008
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Anopheles dirus species B glutathione S-transferases 1-3
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
1JLV is a Single protein structure of sequence from Anopheles cracens with as ligand. 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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