1v2a
From Proteopedia
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| - | [[Image:1v2a.jpg|left|200px]] | + | [[Image:1v2a.jpg|left|200px]] |
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| - | '''Glutathione S-transferase 1-6 from Anopheles dirus species B''' | + | {{Structure |
| + | |PDB= 1v2a |SIZE=350|CAPTION= <scene name='initialview01'>1v2a</scene>, resolution 2.15Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=GTS:GLUTATHIONE SULFONIC ACID'>GTS</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= AdGST1-6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7168 Anopheles dirus]) | ||
| + | }} | ||
| + | |||
| + | '''Glutathione S-transferase 1-6 from Anopheles dirus species B''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1V2A is a [ | + | 1V2A is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Anopheles_dirus Anopheles dirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V2A OCA]. |
==Reference== | ==Reference== | ||
| - | Identification, characterization and structure of a new Delta class glutathione transferase isoenzyme., Udomsinprasert R, Pongjaroenkit S, Wongsantichon J, Oakley AJ, Prapanthadara LA, Wilce MC, Ketterman AJ, Biochem J. 2005 Jun 15;388(Pt 3):763-71. PMID:[http:// | + | Identification, characterization and structure of a new Delta class glutathione transferase isoenzyme., Udomsinprasert R, Pongjaroenkit S, Wongsantichon J, Oakley AJ, Prapanthadara LA, Wilce MC, Ketterman AJ, Biochem J. 2005 Jun 15;388(Pt 3):763-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15717864 15717864] |
[[Category: Anopheles dirus]] | [[Category: Anopheles dirus]] | ||
[[Category: Glutathione transferase]] | [[Category: Glutathione transferase]] | ||
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[[Category: glutathione]] | [[Category: glutathione]] | ||
[[Category: glutathione s-transferase]] | [[Category: glutathione s-transferase]] | ||
| - | [[Category: | + | [[Category: xenobiotic]] |
| - | ''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 14:39:53 2008'' |
Revision as of 12:39, 20 March 2008
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| , resolution 2.15Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | AdGST1-6 (Anopheles dirus) | ||||||
| Activity: | Glutathione transferase, with EC number 2.5.1.18 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Glutathione S-transferase 1-6 from Anopheles dirus species B
Overview
The insect GST (glutathione transferase) supergene family encodes a varied group of proteins belonging to at least six individual classes. Interest in insect GSTs has focused on their role in conferring insecticide resistance. Previously from the mosquito malaria vector Anopheles dirus, two genes encoding five Delta class GSTs have been characterized for structural as well as enzyme activities. We have obtained a new Delta class GST gene and isoenzyme from A. dirus, which we name adGSTD5-5. The adGSTD5-5 isoenzyme was identified and was only detectably expressed in A. dirus adult females. A putative promoter analysis suggests that this GST has an involvement in oogenesis. The enzyme displayed little activity for classical GST substrates, although it possessed the greatest activity for DDT [1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane] observed for Delta GSTs. However, GST activity was inhibited or enhanced in the presence of various fatty acids, suggesting that the enzyme may be modulated by fatty acids. We obtained a crystal structure for adGSTD5-5 and compared it with other Delta GSTs, which showed that adGSTD5-5 possesses an elongated and more polar active-site topology.
About this Structure
1V2A is a Single protein structure of sequence from Anopheles dirus. Full crystallographic information is available from OCA.
Reference
Identification, characterization and structure of a new Delta class glutathione transferase isoenzyme., Udomsinprasert R, Pongjaroenkit S, Wongsantichon J, Oakley AJ, Prapanthadara LA, Wilce MC, Ketterman AJ, Biochem J. 2005 Jun 15;388(Pt 3):763-71. PMID:15717864
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