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1tpl

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[[Image:1tpl.gif|left|200px]]
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{{STRUCTURE_1tpl| PDB=1tpl | SCENE= }}
{{STRUCTURE_1tpl| PDB=1tpl | SCENE= }}
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'''THE THREE-DIMENSIONAL STRUCTURE OF TYROSINE PHENOL-LYASE'''
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===THE THREE-DIMENSIONAL STRUCTURE OF TYROSINE PHENOL-LYASE===
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==Overview==
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Tyrosine phenol-lyase (EC 4.1.99.2) from Citrobacter freundii has been cloned and the primary sequence deduced from the DNA sequence. From the BrCN digest of the NaBH4-reduced holoenzyme, five peptides were purified and sequenced. The amino acid sequences of the peptides agreed with the corresponding parts of the tyrosine phenol-lyase sequence obtained from the gene structure. K257 is the pyridoxal 5'-phosphate binding residue. Assisted by the sequence data, the crystal structure of apotyrosine phenol-lyase, a pyridoxal 5'-phosphate-dependent enzyme, has been refined to an R-factor of 16.2% at 2.3-A resolution using synchrotron radiation diffraction data. The tetrameric molecule has 222 symmetry, with one of the axes coincident with the crystallographic 2-fold symmetry axis of the crystal which belongs to the space group P2(1)2(1)2 with a = 76.0 A, b = 138.3 A, and c = 93.5 A. Each subunit comprises 14 alpha-helices and 16 beta-strands, which fold into a small and a large domain. The coenzyme-binding lysine residue is located at the interface between the large and small domains of one subunit and the large domain of a crystallographically related subunit. The fold of the large, pyridoxal 5'-phosphate binding domain and the location of the active site are similar to that found in aminotransferases. Most of the residues which participate in binding of pyridoxal 5'-phosphate in aminotransferases are conserved in the structure of tyrosine phenol-lyase. Two dimers of tyrosine phenol-lyase, each of which has a domain architecture similar to that found in aspartate aminotransferases, are bound together through a hydrophobic cluster in the center of the molecule and intertwined N-terminal arms.
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(as it appears on PubMed at http://www.pubmed.gov), where 7916622 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7916622}}
==About this Structure==
==About this Structure==
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[[Category: Harutyunyan, E.]]
[[Category: Harutyunyan, E.]]
[[Category: Wilson, K.]]
[[Category: Wilson, K.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:13:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:29:43 2008''

Revision as of 13:29, 29 July 2008

Image:1tpl.png

Template:STRUCTURE 1tpl

THE THREE-DIMENSIONAL STRUCTURE OF TYROSINE PHENOL-LYASE

Template:ABSTRACT PUBMED 7916622

About this Structure

1TPL is a Single protein structure. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of tyrosine phenol-lyase., Antson AA, Demidkina TV, Gollnick P, Dauter Z, von Tersch RL, Long J, Berezhnoy SN, Phillips RS, Harutyunyan EH, Wilson KS, Biochemistry. 1993 Apr 27;32(16):4195-206. PMID:7916622

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