1v2a

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|PDB= 1v2a |SIZE=350|CAPTION= <scene name='initialview01'>1v2a</scene>, resolution 2.15&Aring;
|PDB= 1v2a |SIZE=350|CAPTION= <scene name='initialview01'>1v2a</scene>, resolution 2.15&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=GTS:GLUTATHIONE SULFONIC ACID'>GTS</scene>
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|LIGAND= <scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene>
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|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]
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|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= AdGST1-6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7168 Anopheles dirus])
|GENE= AdGST1-6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7168 Anopheles dirus])
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|DOMAIN=
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|RELATEDENTRY=[[1jlv|1JLV]], [[1jlw|1JLW]], [[1r5a|1R5A]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v2a OCA], [http://www.ebi.ac.uk/pdbsum/1v2a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v2a RCSB]</span>
}}
}}
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Oakley, A J.]]
[[Category: Oakley, A J.]]
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[[Category: GTS]]
 
[[Category: detoxification]]
[[Category: detoxification]]
[[Category: glutathione]]
[[Category: glutathione]]
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[[Category: xenobiotic]]
[[Category: xenobiotic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:39:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:18:26 2008''

Revision as of 21:18, 30 March 2008


PDB ID 1v2a

Drag the structure with the mouse to rotate
, resolution 2.15Å
Ligands:
Gene: AdGST1-6 (Anopheles dirus)
Activity: Glutathione transferase, with EC number 2.5.1.18
Related: 1JLV, 1JLW, 1R5A


Resources: FirstGlance, OCA, PDBsum, RCSB
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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