3fyg
From Proteopedia
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Revision as of 15:40, 30 October 2007
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CRYSTAL STRUCTURE OF TETRADECA-(3-FLUOROTYROSYL)-GLUTATHIONE S-TRANSFERASE
Overview
The structure of the tetradeca-(3-fluorotyrosyl) M1-1 GSH transferase, (3-FTyr GSH transferase), a protein in which tyrosine residues are, globally substituted by 3-fluorotyrosines has been determined at 2.2 A, resolution. This variant was produced to study the effect on the enzymatic, mechanism and the structure was undertaken to assess how the presence of, the 3-fluorotyrosyl residue influences the protein conformation and hence, its function. Although fluorinated amino acid residues have frequently, been used in biochemical and NMR investigations of proteins, no structure, of a protein that has been globally substituted with a fluorinated amino, acid has previously been reported. Thus, this structure represents the, first crystal structure of such a protein containing a library of 14 ... [(full description)]
About this Structure
3FYG is a [Single protein] structure of sequence from [Rattus norvegicus] with GPR as [ligand]. Active as [Glutathione transferase], with EC number [2.5.1.18]. Structure known Active Sites: AVA and AVB. Full crystallographic information is available from [OCA].
Reference
Conformational changes in the crystal structure of rat glutathione transferase M1-1 with global substitution of 3-fluorotyrosine for tyrosine., Xiao G, Parsons JF, Tesh K, Armstrong RN, Gilliland GL, J Mol Biol. 1998 Aug 14;281(2):323-39. PMID:9698551
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