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TitleStructures of apo- and holo-tyrosine phenol-lyase reveal a catalytically critical closed conformation and suggest a mechanism for activation by K+ ions
Journal, issue, pagesBiochemistry, Vol. 45, Page 7544-7552, Year 2006
Publish dateNov 10, 2005 (structure data deposition date)
AuthorsMilic, D. / Matkovic-Calogovic, D. / Demidkina, T.V. / Kulikova, V.V. / Sinitzina, N.I. / Antson, A.A.
External linksBiochemistry / PubMed:16768450
MethodsX-ray diffraction
Resolution1.85 - 1.9 Å
Structure data

PDB-2ez1:
Holo tyrosine phenol-lyase from Citrobacter freundii at pH 8.0
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-2ez2:
Apo tyrosine phenol-lyase from Citrobacter freundii at pH 8.0
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-K:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

Source
  • citrobacter freundii (bacteria)
KeywordsLYASE / lyase; PLP-dependent enzyme; pyridoxal-5'-phosphate; domain closure

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