1gsy
From Proteopedia
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| - | [[Image:1gsy.gif|left|200px]]<br /> | + | [[Image:1gsy.gif|left|200px]]<br /><applet load="1gsy" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1gsy" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1gsy, resolution 2.44Å" /> | caption="1gsy, resolution 2.44Å" /> | ||
'''GLUTATHIONE S-TRANSFERASE YFYF, CLASS PI, COMPLEXED WITH GLUTATHIONE'''<br /> | '''GLUTATHIONE S-TRANSFERASE YFYF, CLASS PI, COMPLEXED WITH GLUTATHIONE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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 GTT 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] | + | 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 GTT 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GSY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:34:28 2007'' |
Revision as of 13:24, 18 December 2007
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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 with GTT as ligand. Active as Glutathione transferase, with EC number 2.5.1.18 Known structural/functional Sites: and . 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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