2tpl Summary

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TYROSINE PHENOL-LYASE FROM CITROBACTER INTERMEDIUS COMPLEX WITH 3-(4'-HYDROXYPHENYL)PROPIONIC ACID, PYRIDOXAL-5'-PHOSPHATE AND CS+ ION

The structure was published by Sundararaju, B., Antson, A.A., Phillips, R.S., et al., Gollnick, P., Dodson, G.G., and Wilson, K.S., in 1997 in a paper entitled "The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 1997.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of TYROSINE PHENOL-LYASE.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homotetramers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A TYROSINE PHENOL-LYASE P31013 (1-456) (TPL_CITFR)search Citrobacter freundiisearch 100% 456 99%
B TYROSINE PHENOL-LYASE P31013 (1-456) (TPL_CITFR)search Citrobacter freundiisearch 100% 456 99%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P31013 (1 - 456) TYROSINE PHENOL-LYASE Citrobacter freundii

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P31013) Beta-eliminating lyasessearch Aspartate Aminotransferase, domain 1search, Type I PLP-dependent aspartate aminotransferase-like (Major domain)search PF01212: Beta-eliminating lyasesearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (P31013) catalytic activitysearch carbon-carbon lyase activitysearch pyridoxal phosphate bindingsearch tyrosine phenol-lyase activitysearch lyase activitysearch cellular amino acid metabolic processsearch tyrosine metabolic processsearch aromatic amino acid family metabolic processsearch

Chain InterPro annotation
A, B Aromatic amino acid beta-eliminating lyase/threonine aldolasesearch Beta-eliminating lyase familysearch Tyrosine phenol-lyasesearch Pyridoxal phosphate-dependent transferase, major region, subdomain 1search Pyridoxal phosphate-dependent transferase, major region, subdomain 2search Pyridoxal phosphate-dependent transferasesearch Tryptophanase, conserved sitesearch