2pvq: Difference between revisions

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[[Image:2pvq.~~jpg~~|left|200px]]

[[Image:2pvq.png|left|200px]]

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~~'''~~Crystal structure of Ochrobactrum anthropi glutathione transferase Cys10Ala mutant with glutathione bound at the H-site~~'''~~

===Crystal structure of Ochrobactrum anthropi glutathione transferase Cys10Ala mutant with glutathione bound at the H-site===

~~==Overview==~~

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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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_18076047}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 18076047 is the PubMed ID number.

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==About this Structure==

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[[Category: Transferase]]

[[Category: Xenobiotics detoxification]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun ~~May 4 13~~:52:29 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:45:15 2008''

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-[[Image:2pvq.jpg|left|200px]]
+{{Seed}}
+[[Image:2pvq.png|left|200px]]
 <!--
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 {{STRUCTURE_2pvq|  PDB=2pvq  |  SCENE=  }}
-'''Crystal structure of Ochrobactrum anthropi glutathione transferase Cys10Ala mutant with glutathione bound at the H-site'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_18076047}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18076047 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18076047}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Transferase]]
 [[Category: Xenobiotics detoxification]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 13:52:29 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:45:15 2008''