1TPL

THE THREE-DIMENSIONAL STRUCTURE OF TYROSINE PHENOL-LYASE

Summary for 1TPL

• Entry DOI: 10.2210/pdb1tpl/pdb
• Descriptor: TYROSINE PHENOL-LYASE, SULFATE ION (3 entities in total)
• Functional Keywords: lyase(carbon-carbon)
• Biological source: Citrobacter intermedius
• Total number of polymer chains: 2
• Total formula weight: 103401.76

Authors

Antson, A.,Demidkina, T.,Dauter, Z.,Harutyunyan, E.,Wilson, K. (deposition date: 1992-11-25, release date: 1993-10-31, Last modification date: 2024-02-14)

Primary citation

Antson, A.A.,Demidkina, T.V.,Gollnick, P.,Dauter, Z.,von Tersch, R.L.,Long, J.,Berezhnoy, S.N.,Phillips, R.S.,Harutyunyan, E.H.,Wilson, K.S.
Three-dimensional structure of tyrosine phenol-lyase.
Biochemistry, 32:4195-4206, 1993

PubMed Abstract: 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.

PubMed: 7916622
DOI: 10.1021/bi00067a006

Experimental method

X-RAY DIFFRACTION (2.3 Å)