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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase.

Tyrosine aminotransferase catalyzes transamination for both dicarboxylic and aromatic amino-acid substrates. The substrate-free Escherichia coli tyrosine aminotransferase (eTAT) bound with the cofactor pyridoxal 5'-phosphate ( PLP) was crystallized in the trigonal space group P3(2). A low-resolution crystal structure of eTAT was determined by molecular-replacement methods. The overall folding of eTAT resembles that of the aspartate aminotransferases, with the two identical subunits forming a dimer in which each monomer binds a PLP molecule via a covalent bond linked to the epsilon-NH(2) group of Lys258. Comparison of the structure of eTAT with those of the open, half-open or closed form of chicken or E. coli aspartate aminotransferases shows the eTAT structure to be in the open conformation.[1]

References

  1. Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase. Ko, T.P., Wu, S.P., Yang, W.Z., Tsai, H., Yuan, H.S. Acta Crystallogr. D Biol. Crystallogr. (1999) [Pubmed]
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