1bay: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1bay.jpg|left|200px]] | [[Image:1bay.jpg|left|200px]] | ||
'''GLUTATHIONE S-TRANSFERASE YFYF CYS 47-CARBOXYMETHYLATED CLASS PI, FREE ENZYME''' | {{Structure | ||
|PDB= 1bay |SIZE=350|CAPTION= <scene name='initialview01'>1bay</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= | |||
|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= | |||
}} | |||
'''GLUTATHIONE S-TRANSFERASE YFYF CYS 47-CARBOXYMETHYLATED CLASS PI, FREE ENZYME''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1BAY is a [ | 1BAY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BAY OCA]. | ||
==Reference== | ==Reference== | ||
The three-dimensional structure of Cys-47-modified mouse liver glutathione S-transferase P1-1. Carboxymethylation dramatically decreases the affinity for glutathione and is associated with a loss of electron density in the alphaB-310B region., Vega MC, Walsh SB, Mantle TJ, Coll M, J Biol Chem. 1998 Jan 30;273(5):2844-50. PMID:[http:// | The three-dimensional structure of Cys-47-modified mouse liver glutathione S-transferase P1-1. Carboxymethylation dramatically decreases the affinity for glutathione and is associated with a loss of electron density in the alphaB-310B region., Vega MC, Walsh SB, Mantle TJ, Coll M, J Biol Chem. 1998 Jan 30;273(5):2844-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9446594 9446594] | ||
[[Category: Glutathione transferase]] | [[Category: Glutathione transferase]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| Line 19: | Line 28: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
''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 10:08:36 2008'' | ||
Revision as of 08:08, 20 March 2008
| |||||||||||||
| 1bay, resolution 2.0Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Activity: | Glutathione transferase, with EC number 2.5.1.18 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
GLUTATHIONE S-TRANSFERASE YFYF CYS 47-CARBOXYMETHYLATED CLASS PI, FREE ENZYME
Overview
The three-dimensional structure of mouse liver glutathione S-transferase P1-1 carboxymethylated at Cys-47 and its complex with S-(p-nitrobenzyl)glutathione have been determined by x-ray diffraction analysis. The structure of the modified enzyme described here is the first structural report for a Pi class glutathione S-transferase with no glutathione, glutathione S-conjugate, or inhibitor bound. It shows that part of the active site area, which includes helix alphaB and helix 310B, is disordered. However, the environment of Tyr-7, an essential residue for the catalytic reaction, remains unchanged. The position of the sulfur atom of glutathione is occupied in the ligand-free enzyme by a water molecule that is at H-bond distance from Tyr-7. We do not find any structural evidence for a tyrosinate form, and therefore our results suggest that Tyr-7 is not acting as a general base abstracting the proton from the thiol group of glutathione. The binding of the inhibitor S-(p-nitrobenzyl)-glutathione to the carboxymethylated enzyme results in a partial restructuring of the disordered area. The modification of Cys-47 sterically hinders structural organization of this region, and although it does not prevent glutathione binding, it significantly reduces the affinity. A detailed kinetic study of the modified enzyme indicates that the carboxymethylation increases the Km for glutathione by 3 orders of magnitude, although the enzyme can function efficiently under saturating conditions.
About this Structure
1BAY is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of Cys-47-modified mouse liver glutathione S-transferase P1-1. Carboxymethylation dramatically decreases the affinity for glutathione and is associated with a loss of electron density in the alphaB-310B region., Vega MC, Walsh SB, Mantle TJ, Coll M, J Biol Chem. 1998 Jan 30;273(5):2844-50. PMID:9446594
Page seeded by OCA on Thu Mar 20 10:08:36 2008
