1jlv: Difference between revisions
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'''Anopheles dirus species B glutathione S-transferases 1-3''' | {{Structure | ||
|PDB= 1jlv |SIZE=350|CAPTION= <scene name='initialview01'>1jlv</scene>, resolution 1.75Å | |||
|SITE= | |||
|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] | |||
|GENE= | |||
}} | |||
'''Anopheles dirus species B glutathione S-transferases 1-3''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1JLV is a [ | 1JLV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Anopheles_cracens Anopheles cracens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JLV OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11604524 11604524] | ||
[[Category: Anopheles cracens]] | [[Category: Anopheles cracens]] | ||
[[Category: Glutathione transferase]] | [[Category: Glutathione transferase]] | ||
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[[Category: gst]] | [[Category: gst]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:05:14 2008'' | ||
Revision as of 10:05, 20 March 2008
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| 1jlv, resolution 1.75Å | |||||||||||||
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| Ligands: | GSH | ||||||||||||
| Activity: | Glutathione transferase, with EC number 2.5.1.18 | ||||||||||||
| 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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