1jlv

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[[Image:1jlv.gif|left|200px]]
[[Image:1jlv.gif|left|200px]]
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{{Structure
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|PDB= 1jlv |SIZE=350|CAPTION= <scene name='initialview01'>1jlv</scene>, resolution 1.75&Aring;
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The line below this paragraph, containing "STRUCTURE_1jlv", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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>
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{{STRUCTURE_1jlv| PDB=1jlv | SCENE= }}
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|RELATEDENTRY=[[1jlv|1JLV]]
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|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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'''Anopheles dirus species B glutathione S-transferases 1-3'''
'''Anopheles dirus species B glutathione S-transferases 1-3'''
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[[Category: Udomsinprasert, R.]]
[[Category: Udomsinprasert, R.]]
[[Category: Wilce, M C.]]
[[Category: Wilce, M C.]]
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[[Category: adgst1-3]]
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[[Category: Adgst1-3]]
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[[Category: glutathione s-transferase]]
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[[Category: Glutathione s-transferase]]
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[[Category: gst]]
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[[Category: Gst]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:23:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:35:32 2008''
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Revision as of 18:23, 2 May 2008

Image:1jlv.gif

Template:STRUCTURE 1jlv

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 Page seeded by OCA on Fri May 2 21:23:00 2008

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