3tat

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[[Image:3tat.jpg|left|200px]]
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{{STRUCTURE_3tat| PDB=3tat | SCENE= }}
{{STRUCTURE_3tat| PDB=3tat | SCENE= }}
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'''TYROSINE AMINOTRANSFERASE FROM E. COLI'''
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===TYROSINE AMINOTRANSFERASE FROM E. COLI===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10417420 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10417420}}
==About this Structure==
==About this Structure==
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[[Category: Aromatic substrate]]
[[Category: Aromatic substrate]]
[[Category: Plp enzyme]]
[[Category: Plp enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:08:15 2008''

Revision as of 10:08, 3 July 2008

Image:3tat.png

Template:STRUCTURE 3tat

TYROSINE AMINOTRANSFERASE FROM E. COLI

Template:ABSTRACT PUBMED 10417420

About this Structure

3TAT is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase., Ko TP, Wu SP, Yang WZ, Tsai H, Yuan HS, Acta Crystallogr D Biol Crystallogr. 1999 Aug;55(Pt 8):1474-7. PMID:10417420

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