1e6b: Difference between revisions

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[[Image:1e6b.jpg|left|200px]]
{{Seed}}
[[Image:1e6b.png|left|200px]]


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{{STRUCTURE_1e6b|  PDB=1e6b  |  SCENE=  }}  
{{STRUCTURE_1e6b|  PDB=1e6b  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF A ZETA CLASS GLUTATHIONE S-TRANSFERASE FROM ARABIDOPSIS THALIANA'''
===CRYSTAL STRUCTURE OF A ZETA CLASS GLUTATHIONE S-TRANSFERASE FROM ARABIDOPSIS THALIANA===




==Overview==
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The cis-trans isomerisation of maleylacetoacetate to fumarylacetoacetate is the penultimate step in the tyrosine/phenylalanine catabolic pathway and has recently been shown to be catalysed by glutathione S-transferase enzymes belonging to the zeta class. Given this primary metabolic role it is unsurprising that zeta class glutathione S-transferases are well conserved over a considerable period of evolution, being found in vertebrates, plants, insects and fungi. The structure of this glutathione S-transferase, cloned from Arabidopsis thaliana, has been solved by single isomorphous replacement with anomalous scattering and refined to a final crystallographic R-factor of 19.6% using data from 25.0 A to 1.65 A. The zeta class enzyme adopts the canonical glutathione S-transferase fold and forms a homodimer with each subunit consisting of 221 residues. In agreement with structures of glutathione S-transferases from the theta and phi classes, a serine residue (Ser17) is present in the active site, at a position that would allow it to stabilise the thiolate anion of glutathione. Site-directed mutagenesis of this residue confirms its importance in catalysis. In addition, the role of a highly conserved cysteine residue (Cys19) present in the active site of the zeta class glutathione S-transferase enzymes is discussed.
The line below this paragraph, {{ABSTRACT_PUBMED_11352584}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_11352584}}


==About this Structure==
==About this Structure==
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[[Category: Thom, R.]]
[[Category: Thom, R.]]
[[Category: Transferase]]
[[Category: Transferase]]
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