1aqv: Difference between revisions
New page: left|200px<br /> <applet load="1aqv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aqv, resolution 1.94Å" /> '''GLUTATHIONE S-TRANS... |
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[[Image:1aqv.gif|left|200px]]<br /> | [[Image:1aqv.gif|left|200px]]<br /><applet load="1aqv" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1aqv" size=" | |||
caption="1aqv, resolution 1.94Å" /> | caption="1aqv, resolution 1.94Å" /> | ||
'''GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH P-BROMOBENZYLGLUTATHIONE'''<br /> | '''GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH P-BROMOBENZYLGLUTATHIONE'''<br /> | ||
==Overview== | ==Overview== | ||
The three-dimensional structure of human class pi glutathione | The three-dimensional structure of human class pi glutathione S-transferase from placenta (hGSTP1-1), a homodimeric enzyme, has been solved by Patterson search methods and refined at 2.8 A resolution to a final crystallographic R-factor of 19.6% (8.0 to 2.8 A resolution). Subunit folding topology, subunit overall structure and subunit association closely resembles the structure of porcine class pi glutathione S-transferase. The binding site of a competitive inhibitor, S-hexylglutathione, is analyzed and the locations of the binding regions for glutathione (G-site) and electrophilic substrates (H-site) are determined. The specific interactions between protein and the inhibitor's glutathione peptide are the same as those observed between glutathione sulfonate and the porcine isozyme. The H-site is located adjacent to the G-site, with the hexyl moiety lying above a segment (residues 8 to 10) connecting strand beta 1 and helix alpha A where it is in hydrophobic contact with Tyr7, Phe8, Val10, Val35 and Tyr106. Catalytic models are discussed on the basis of the molecular structure. | ||
==About this Structure== | ==About this Structure== | ||
1AQV 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 MES 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] Full crystallographic information is available from [http:// | 1AQV 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=MES:'>MES</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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AQV OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fahl, W | [[Category: Fahl, W E.]] | ||
[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
[[Category: Manoharan, T | [[Category: Manoharan, T H.]] | ||
[[Category: Prade, L.]] | [[Category: Prade, L.]] | ||
[[Category: Reuter, W.]] | [[Category: Reuter, W.]] | ||
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[[Category: complex (transferase/peptide)]] | [[Category: complex (transferase/peptide)]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:47:21 2008'' | ||
Revision as of 12:47, 21 February 2008
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GLUTATHIONE S-TRANSFERASE IN COMPLEX WITH P-BROMOBENZYLGLUTATHIONE
OverviewOverview
The three-dimensional structure of human class pi glutathione S-transferase from placenta (hGSTP1-1), a homodimeric enzyme, has been solved by Patterson search methods and refined at 2.8 A resolution to a final crystallographic R-factor of 19.6% (8.0 to 2.8 A resolution). Subunit folding topology, subunit overall structure and subunit association closely resembles the structure of porcine class pi glutathione S-transferase. The binding site of a competitive inhibitor, S-hexylglutathione, is analyzed and the locations of the binding regions for glutathione (G-site) and electrophilic substrates (H-site) are determined. The specific interactions between protein and the inhibitor's glutathione peptide are the same as those observed between glutathione sulfonate and the porcine isozyme. The H-site is located adjacent to the G-site, with the hexyl moiety lying above a segment (residues 8 to 10) connecting strand beta 1 and helix alpha A where it is in hydrophobic contact with Tyr7, Phe8, Val10, Val35 and Tyr106. Catalytic models are discussed on the basis of the molecular structure.
About this StructureAbout this Structure
1AQV is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Glutathione transferase, with EC number 2.5.1.18 Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution., Reinemer P, Dirr HW, Ladenstein R, Huber R, Lo Bello M, Federici G, Parker MW, J Mol Biol. 1992 Sep 5;227(1):214-26. PMID:1522586
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