1jlv
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene> | |LIGAND= <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene> | ||
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1jlv|1JLV]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jlv OCA], [http://www.ebi.ac.uk/pdbsum/1jlv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jlv RCSB]</span> | ||
}} | }} | ||
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[[Category: Udomsinprasert, R.]] | [[Category: Udomsinprasert, R.]] | ||
[[Category: Wilce, M C.]] | [[Category: Wilce, M C.]] | ||
| - | [[Category: GSH]] | ||
[[Category: adgst1-3]] | [[Category: adgst1-3]] | ||
[[Category: glutathione s-transferase]] | [[Category: glutathione s-transferase]] | ||
[[Category: gst]] | [[Category: gst]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:35:32 2008'' |
Revision as of 18:35, 30 March 2008
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| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Glutathione transferase, with EC number 2.5.1.18 | ||||||
| Related: | 1JLV
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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