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1gsy

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[[Image:1gsy.gif|left|200px]]<br /><applet load="1gsy" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1gsy.gif|left|200px]]
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caption="1gsy, resolution 2.44&Aring;" />
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'''GLUTATHIONE S-TRANSFERASE YFYF, CLASS PI, COMPLEXED WITH GLUTATHIONE'''<br />
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{{Structure
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|PDB= 1gsy |SIZE=350|CAPTION= <scene name='initialview01'>1gsy</scene>, resolution 2.44&Aring;
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|SITE= <scene name='pdbsite=GAS:ASP+98+Belongs+To+Monomer+B'>GAS</scene> and <scene name='pdbsite=GBS:ASP+98+Belongs+To+Monomer+A'>GBS</scene>
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|LIGAND= <scene name='pdbligand=GTT:GLUTATHIONE'>GTT</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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|GENE=
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}}
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'''GLUTATHIONE S-TRANSFERASE YFYF, CLASS PI, COMPLEXED WITH GLUTATHIONE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1GSY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=GTT:'>GTT</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] Known structural/functional Sites: <scene name='pdbsite=GAS:ASP+98+Belongs+To+Monomer+B'>GAS</scene> and <scene name='pdbsite=GBS:ASP+98+Belongs+To+Monomer+A'>GBS</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GSY OCA].
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1GSY 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=1GSY OCA].
==Reference==
==Reference==
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Molecular structure at 1.8 A of mouse liver class pi glutathione S-transferase complexed with S-(p-nitrobenzyl)glutathione and other inhibitors., Garcia-Saez I, Parraga A, Phillips MF, Mantle TJ, Coll M, J Mol Biol. 1994 Apr 1;237(3):298-314. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8145243 8145243]
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Molecular structure at 1.8 A of mouse liver class pi glutathione S-transferase complexed with S-(p-nitrobenzyl)glutathione and other inhibitors., Garcia-Saez I, Parraga A, Phillips MF, Mantle TJ, Coll M, J Mol Biol. 1994 Apr 1;237(3):298-314. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8145243 8145243]
[[Category: Glutathione transferase]]
[[Category: Glutathione transferase]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:53:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:27:30 2008''

Revision as of 09:27, 20 March 2008

Image:1gsy.gif


PDB ID 1gsy

Drag the structure with the mouse to rotate
, resolution 2.44Å
Sites: and
Ligands:
Activity: Glutathione transferase, with EC number 2.5.1.18
Coordinates: save as pdb, mmCIF, xml



GLUTATHIONE S-TRANSFERASE YFYF, CLASS PI, COMPLEXED WITH GLUTATHIONE


Overview

The three-dimensional crystal structure of pi class glutathione S-transferase YfYf from mouse liver complexed with the inhibitor S-(p-nitrobenzyl)glutathione has been determined at 1.8 A resolution by X-ray diffraction. In addition two complexes with glutathione sulphonic acid and S-hexylglutathione have been determined at resolutions of 1.9 and 2.2 A, respectively. The high resolution of the S-(p-nitrobenzyl)glutathione complex allows a detailed analysis of the active site including the hydrophobic (H-) subsite. The nitrobenzyl moiety occupies a hydrophobic pocket with its aromatic ring sandwiched between Phe8 and the hydroxyl group of Tyr108. An insertion of two residues Gly41 and Leu42, with respect to the pig enzyme, splits helix alpha B into an alpha-helix and a 3(10) helix. Water bridges between carbonyl oxygen atoms of the alpha-helix at its C terminus and the amide NH groups of the 3(10) helix at its N terminus provide structural continuity between these two secondary elements. Tyr7 appears to be the only residue close to the sulphur atom of glutathione, while three conserved water molecules lie in the surrounding area in all complexes. The enzyme mechanism is discussed on the basis of the structural analysis.

About this Structure

1GSY is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Molecular structure at 1.8 A of mouse liver class pi glutathione S-transferase complexed with S-(p-nitrobenzyl)glutathione and other inhibitors., Garcia-Saez I, Parraga A, Phillips MF, Mantle TJ, Coll M, J Mol Biol. 1994 Apr 1;237(3):298-314. PMID:8145243

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