This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1gse

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1gse.gif|left|200px]]<br /><applet load="1gse" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1gse.gif|left|200px]]
-
caption="1gse, resolution 2.0&Aring;" />
+
 
-
'''GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH AN ETHACRYNIC ACID GLUTATHIONE CONJUGATE (MUTANT R15K)'''<br />
+
{{Structure
 +
|PDB= 1gse |SIZE=350|CAPTION= <scene name='initialview01'>1gse</scene>, resolution 2.0&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=GTT:GLUTATHIONE'>GTT</scene>, <scene name='pdbligand=EAA:ETHACRYNIC+ACID'>EAA</scene> and <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</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=
 +
}}
 +
 
 +
'''GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH AN ETHACRYNIC ACID GLUTATHIONE CONJUGATE (MUTANT R15K)'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1GSE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=GTT:'>GTT</scene>, <scene name='pdbligand=EAA:'>EAA</scene> and <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1GSE OCA].
+
1GSE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GSE OCA].
==Reference==
==Reference==
-
Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate., Cameron AD, Sinning I, L'Hermite G, Olin B, Board PG, Mannervik B, Jones TA, Structure. 1995 Jul 15;3(7):717-27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8591048 8591048]
+
Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate., Cameron AD, Sinning I, L'Hermite G, Olin B, Board PG, Mannervik B, Jones TA, Structure. 1995 Jul 15;3(7):717-27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8591048 8591048]
[[Category: Glutathione transferase]]
[[Category: Glutathione transferase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
Line 21: Line 30:
[[Category: a1-1]]
[[Category: a1-1]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:53:26 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:27:15 2008''

Revision as of 09:27, 20 March 2008


PDB ID 1gse

Drag the structure with the mouse to rotate
, resolution 2.0Å
Ligands: , and
Activity: Glutathione transferase, with EC number 2.5.1.18
Coordinates: save as pdb, mmCIF, xml



GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH AN ETHACRYNIC ACID GLUTATHIONE CONJUGATE (MUTANT R15K)


Overview

BACKGROUND: Glutathione transferases (GSTs) constitute a family of isoenzymes that catalyze the conjugation of the tripeptide glutathione with a wide variety of hydrophobic compounds bearing an electrophilic functional group. Recently, a number of X-ray structures have been reported which have defined both the glutathione- and the substrate-binding sites in these enzymes. The structure of the glutathione-free enzyme from a mammalian source has not, however, been reported previously. RESULTS: We have solved structures of a human alpha-class GST, isoenzyme A1-1, both in the unliganded form and in complexes with the inhibitor ethacrynic acid and its glutathione conjugate. These structures have been refined to resolutions of 2.5 A, 2.7 A and 2.0 A respectively. Both forms of the inhibitor are clearly present in the associated electron density. CONCLUSIONS: The major differences among the three structures reported here involve the C-terminal alpha-helix, which is a characteristic of the alpha-class enzyme. This helix forms a lid over the active site when the hydrophobic substrate binding site (H-site) is occupied but it is otherwise disordered. Ethacrynic acid appears to bind in a non-productive mode in the absence of the coenzyme glutathione.

About this Structure

1GSE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate., Cameron AD, Sinning I, L'Hermite G, Olin B, Board PG, Mannervik B, Jones TA, Structure. 1995 Jul 15;3(7):717-27. PMID:8591048

Page seeded by OCA on Thu Mar 20 11:27:15 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools