2f8f

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2f8f.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2f8f.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2f8f| PDB=2f8f | SCENE= }}
{{STRUCTURE_2f8f| PDB=2f8f | SCENE= }}
-
'''Crystal structure of the Y10F mutant of the gluathione s-transferase from schistosoma haematobium'''
+
===Crystal structure of the Y10F mutant of the gluathione s-transferase from schistosoma haematobium===
-
==Overview==
+
<!--
-
During turnover, the catalytic tyrosine residue (Tyr10) of the sigma class Schistosoma haematobium wild-type glutathione-S-transferase is expected to switch alternately in and out of the reduced glutathione-binding site (G-site). The Tyrout10 conformer forms a pi-cation interaction with the guanidinium group of Arg21. As in other similar glutathione-S-transferases, the catalytic Tyr has a low pKa of 7.2. In order to investigate the catalytic role of Tyr10, and the structural and functional roles of Arg21, we carried out structural studies on two Arg21 mutants (R21L and R21Q) and a Tyr10 mutant, Y10F. Our crystallographic data for the two Arg21 mutants indicate that only the Tyrout10 conformation is populated, thereby excluding a role of Arg21 in the stabilisation of the out conformation. However, Arg21 was confirmed to be catalytically important and essential for the low pKa of Tyr10. Upon comparison with structural data generated for reduced glutathione-bound and inhibitor-bound wild-type enzymes, it was observed that the orientations of Tyr10 and Arg35 are concerted and that, upon ligand binding, minor rearrangements occur within conserved residues in the active site loop. These rearrangements are coupled to quaternary rigid-body movements at the dimer interface and alterations in the localisation and structural order of the C-terminal domain.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16777141}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16777141 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16777141}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Protein_gtt complex]]
[[Category: Protein_gtt complex]]
[[Category: Thioredoxin fold]]
[[Category: Thioredoxin fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:35:16 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:43:01 2008''

Revision as of 23:43, 28 July 2008

Template:STRUCTURE 2f8f

Crystal structure of the Y10F mutant of the gluathione s-transferase from schistosoma haematobium

Template:ABSTRACT PUBMED 16777141

About this Structure

2F8F is a Single protein structure of sequence from Schistosoma haematobium. Full crystallographic information is available from OCA.

Reference

Probing the mechanism of GSH activation in Schistosoma haematobium glutathione-S-transferase by site-directed mutagenesis and X-ray crystallography., Baiocco P, Gourlay LJ, Angelucci F, Fontaine J, Herve M, Miele AE, Trottein F, Brunori M, Bellelli A, J Mol Biol. 2006 Jul 14;360(3):678-89. Epub 2006 Jun 2. PMID:16777141

Page seeded by OCA on Tue Jul 29 02:43:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools