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| - | [[Image:1tpl.gif|left|200px]] | + | {{Seed}} |
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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'''
| + | ===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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_7916622}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 7916622 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_7916622}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Harutyunyan, E.]] | | [[Category: Harutyunyan, E.]] |
| | [[Category: Wilson, K.]] | | [[Category: Wilson, K.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:13:33 2008'' | + | |
| | + | ''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
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
Page seeded by OCA on Tue Jul 29 16:29:43 2008
