2caq
From Proteopedia
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STRUCTURE OF R21L MUTANT OF SH28GST IN COMPLEX WITH GSH
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 ... [(full description)]
About this Structure
2CAQ is a [Single protein] structure of sequence from [Schistosoma haematobium] with GSW, PG4 and BME as [ligands]. Active as [Glutathione transferase], with EC number [2.5.1.18]. Structure known Active Site: AC1. 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
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