3tat: Difference between revisions
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==Overview== | ==Overview== | ||
Tyrosine aminotransferase catalyzes transamination for both dicarboxylic | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ko, T | [[Category: Ko, T P.]] | ||
[[Category: Tsai, H.]] | [[Category: Tsai, H.]] | ||
[[Category: Wu, S | [[Category: Wu, S P.]] | ||
[[Category: Yang, W | [[Category: Yang, W Z.]] | ||
[[Category: Yuan, H | [[Category: Yuan, H S.]] | ||
[[Category: PLP]] | [[Category: PLP]] | ||
[[Category: aminotransferase]] | [[Category: aminotransferase]] | ||
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[[Category: plp enzyme]] | [[Category: plp enzyme]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:11:31 2008'' | ||