2pvq
From Proteopedia
(New page: 200px<br /><applet load="2pvq" size="350" color="white" frame="true" align="right" spinBox="true" caption="2pvq, resolution 1.803Å" /> '''Crystal structure o...) |
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==Overview== | ==Overview== | ||
| - | The role of the evolutionarily conserved residue Cys10 in Ochrobactrum | + | The role of the evolutionarily conserved residue Cys10 in Ochrobactrum anthropi glutathione transferase (OaGST) has been examined by replacing it with an alanine. A double mutant C10A/S11A was also prepared. The effect of the replacements on the coniugating and thiotransferase activities, and on the thermal and chemical stability of the enzyme was analyzed. Our data support the view that in OaGST, in contrast with other beta class GSTs that display significant differences in the glutathione-binding site, Cys10 is a key residue for glutathione coniugating activity. Furthermore, analysis of the OaGST-Cys10Ala structure, crystallized in the presence of glutathione, reveals that this mutation causes a switch between the high-affinity G-site and a low-affinity H-site where hydrophobic cosubstrates bind and where we observe the presence of an unexpected glutathione. Proteins 2008. (c) 2007 Wiley-Liss, Inc. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site., Allocati N, Federici L, Masulli M, Favaloro B, Di Ilio C, Proteins. 2007 Dec 12;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18076047 18076047] | + | Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site., Allocati N, Federici L, Masulli M, Favaloro B, Di Ilio C, Proteins. 2007 Dec 12;71(1):16-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18076047 18076047] |
[[Category: Glutathione transferase]] | [[Category: Glutathione transferase]] | ||
[[Category: Ochrobactrum anthropi]] | [[Category: Ochrobactrum anthropi]] | ||
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[[Category: Favaloro, B.]] | [[Category: Favaloro, B.]] | ||
[[Category: Federici, L.]] | [[Category: Federici, L.]] | ||
| - | [[Category: Ilio, C | + | [[Category: Ilio, C Di.]] |
[[Category: Masulli, M.]] | [[Category: Masulli, M.]] | ||
[[Category: GTT]] | [[Category: GTT]] | ||
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[[Category: xenobiotics detoxification]] | [[Category: xenobiotics detoxification]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:33:30 2008'' |
Revision as of 16:33, 21 February 2008
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Crystal structure of Ochrobactrum anthropi glutathione transferase Cys10Ala mutant with glutathione bound at the H-site
Overview
The role of the evolutionarily conserved residue Cys10 in Ochrobactrum anthropi glutathione transferase (OaGST) has been examined by replacing it with an alanine. A double mutant C10A/S11A was also prepared. The effect of the replacements on the coniugating and thiotransferase activities, and on the thermal and chemical stability of the enzyme was analyzed. Our data support the view that in OaGST, in contrast with other beta class GSTs that display significant differences in the glutathione-binding site, Cys10 is a key residue for glutathione coniugating activity. Furthermore, analysis of the OaGST-Cys10Ala structure, crystallized in the presence of glutathione, reveals that this mutation causes a switch between the high-affinity G-site and a low-affinity H-site where hydrophobic cosubstrates bind and where we observe the presence of an unexpected glutathione. Proteins 2008. (c) 2007 Wiley-Liss, Inc.
About this Structure
2PVQ is a Single protein structure of sequence from Ochrobactrum anthropi with and as ligands. Active as Glutathione transferase, with EC number 2.5.1.18 Full crystallographic information is available from OCA.
Reference
Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site., Allocati N, Federici L, Masulli M, Favaloro B, Di Ilio C, Proteins. 2007 Dec 12;71(1):16-23. PMID:18076047
Page seeded by OCA on Thu Feb 21 18:33:30 2008
