1v2a
From Proteopedia
(New page: 200px<br /><applet load="1v2a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v2a, resolution 2.15Å" /> '''Glutathione S-transf...) |
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| - | [[Image:1v2a.jpg|left|200px]]<br /><applet load="1v2a" size=" | + | [[Image:1v2a.jpg|left|200px]]<br /><applet load="1v2a" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1v2a, resolution 2.15Å" /> | caption="1v2a, resolution 2.15Å" /> | ||
'''Glutathione S-transferase 1-6 from Anopheles dirus species B'''<br /> | '''Glutathione S-transferase 1-6 from Anopheles dirus species B'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The insect GST (glutathione transferase) supergene family encodes a varied | + | 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== | ==About this Structure== | ||
| - | 1V2A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anopheles_dirus Anopheles dirus] with GTS 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:// | + | 1V2A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anopheles_dirus Anopheles dirus] with <scene name='pdbligand=GTS:'>GTS</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=1V2A OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Glutathione transferase]] | [[Category: Glutathione transferase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Oakley, A | + | [[Category: Oakley, A J.]] |
[[Category: GTS]] | [[Category: GTS]] | ||
[[Category: detoxification]] | [[Category: detoxification]] | ||
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[[Category: xenobiotics]] | [[Category: xenobiotics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:30:42 2008'' |
Revision as of 13:30, 21 February 2008
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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 with as ligand. Active as Glutathione transferase, with EC number 2.5.1.18 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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