1tpl
From Proteopedia
(New page: 200px<br /><applet load="1tpl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tpl, resolution 2.3Å" /> '''THE THREE-DIMENSIONAL...) |
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| - | [[Image:1tpl.gif|left|200px]]<br /><applet load="1tpl" size=" | + | [[Image:1tpl.gif|left|200px]]<br /><applet load="1tpl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tpl, resolution 2.3Å" /> | caption="1tpl, resolution 2.3Å" /> | ||
'''THE THREE-DIMENSIONAL STRUCTURE OF TYROSINE PHENOL-LYASE'''<br /> | '''THE THREE-DIMENSIONAL STRUCTURE OF TYROSINE PHENOL-LYASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Tyrosine phenol-lyase (EC 4.1.99.2) from Citrobacter freundii has been | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1TPL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Tyrosine_phenol-lyase Tyrosine phenol-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.99.2 4.1.99.2] Full crystallographic information is available from [http:// | + | 1TPL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Tyrosine_phenol-lyase Tyrosine phenol-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.99.2 4.1.99.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TPL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: lyase(carbon-carbon)]] | [[Category: lyase(carbon-carbon)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:16:01 2008'' |
Revision as of 13:16, 21 February 2008
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THE THREE-DIMENSIONAL STRUCTURE OF TYROSINE PHENOL-LYASE
Overview
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.
About this Structure
1TPL is a Single protein structure of sequence from [1] with as ligand. Active as Tyrosine phenol-lyase, with EC number 4.1.99.2 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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