2nto
From Proteopedia
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'''Structure of the Glutathione Transferase from Ochrobactrum anthropi in complex with glutathione''' | '''Structure of the Glutathione Transferase from Ochrobactrum anthropi in complex with glutathione''' | ||
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[[Category: Federici, L.]] | [[Category: Federici, L.]] | ||
[[Category: Matteo, A Di.]] | [[Category: Matteo, A Di.]] | ||
| - | [[Category: | + | [[Category: C-terminal all helical domain]] |
| - | [[Category: | + | [[Category: N-terminal alpha+beta domain]] |
| - | [[Category: | + | [[Category: Transferase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:53:57 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:54, 4 May 2008
Structure of the Glutathione Transferase from Ochrobactrum anthropi in complex with glutathione
Overview
GSTs (glutathione transferases) are a multifunctional group of enzymes, widely distributed and involved in cellular detoxification processes. In the xenobiotic-degrading bacterium Ochrobactrum anthropi, GST is overexpressed in the presence of toxic concentrations of aromatic compounds such as 4-chlorophenol and atrazine. We have determined the crystal structure of the GST from O. anthropi (OaGST) in complex with GSH. Like other bacterial GSTs, OaGST belongs to the Beta class and shows a similar binding pocket for GSH. However, in contrast with the structure of Proteus mirabilis GST, GSH is not covalently bound to Cys10, but is present in the thiolate form. In our investigation of the structural basis for GSH stabilization, we have identified a conserved network of hydrogen-bond interactions, mediated by the presence of a structural water molecule that links Ser11 to Glu198. Partial disruption of this network, by mutagenesis of Ser11 to alanine, increases the K(m) for GSH 15-fold and decreases the catalytic efficiency 4-fold, even though Ser11 is not involved in GSH binding. Thermal- and chemical-induced unfolding studies point to a global effect of the mutation on the stability of the protein and to a central role of these residues in zippering the terminal helix of the C-terminal domain to the starting helix of the N-terminal domain.
About this Structure
2NTO is a Single protein structure of sequence from Ochrobactrum anthropi. Full crystallographic information is available from OCA.
Reference
Role of Ser11 in the stabilization of the structure of Ochrobactrum anthropi glutathione transferase., Federici L, Masulli M, Bonivento D, Di Matteo A, Gianni S, Favaloro B, Di Ilio C, Allocati N, Biochem J. 2007 Apr 15;403(2):267-74. PMID:17223798 Page seeded by OCA on Sun May 4 09:53:57 2008
