We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2pvq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2pvq.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2pvq.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2pvq| PDB=2pvq | SCENE= }}
{{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==
==About this Structure==
Line 32: Line 36:
[[Category: Transferase]]
[[Category: Transferase]]
[[Category: Xenobiotics detoxification]]
[[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''

Revision as of 11:45, 27 July 2008

Image:2pvq.png

Template:STRUCTURE 2pvq

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

Template:ABSTRACT PUBMED 18076047

About this Structure

2PVQ is a Single protein structure of sequence from Ochrobactrum anthropi. 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 Sun Jul 27 14:45:15 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2pvq"
Personal tools