3tat
From Proteopedia
(New page: 200px<br /> <applet load="3tat" size="450" color="white" frame="true" align="right" spinBox="true" caption="3tat, resolution 3.5Å" /> '''TYROSINE AMINOTRANSF...) |
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==About this Structure== | ==About this Structure== | ||
| - | 3TAT is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with PLP as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.57 2.6.1.57]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3TAT OCA]]. | + | 3TAT is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with PLP as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Aromatic-amino-acid_transaminase Aromatic-amino-acid transaminase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.57 2.6.1.57]]. Structure known Active Sites: PBA, PBB, PBC, PBD, PBE and PBF. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3TAT OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10417420 10417420] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10417420 10417420] | ||
| + | [[Category: Aromatic-amino-acid transaminase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: plp enzyme]] | [[Category: plp enzyme]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:01:51 2007'' |
Revision as of 10:57, 30 October 2007
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TYROSINE AMINOTRANSFERASE FROM E. COLI
Overview
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 ... [(full description)]
About this Structure
3TAT is a [Single protein] structure of sequence from [Escherichia coli] with PLP as [ligand]. Active as [Aromatic-amino-acid transaminase], with EC number [2.6.1.57]. Structure known Active Sites: PBA, PBB, PBC, PBD, PBE and PBF. 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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