The polypeptide chain fold in tyrosine phenol-lyase, a pyridoxal-5′-phosphate-dependent enzyme
| Autor: | Keith S. Wilson, Michail N. Isupov, Alfred A. Antson, B. V. Strokopytov, E.H. Harutyunyan, Garib N. Murshudov, Howard Terry, Zbigniew Dauter, Tatyana V. Demidkina, Dmitry G. Vassylyev |
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| Rok vydání: | 1992 |
| Předmět: |
Tyrosine phenol lyase
Chemical Phenomena Macromolecular Substances Protein Conformation Stereochemistry Protein subunit Biophysics Tyrosine phenol-lyase Biochemistry chemistry.chemical_compound Citrobacter X-Ray Diffraction Structural Biology Genetics Molecule Pyridoxal phosphate Tyrosine Phenol-Lyase Molecular Biology chemistry.chemical_classification Polypeptide chain fold biology Chemistry Physical Bacterial Cell Biology biology.organism_classification Protein tertiary structure Citrobacter freundii Crystallography Enzyme chemistry Pyridoxal Phosphate X-ray crystallography Crystallization X-ray analysis |
| Zdroj: | FEBS Letters. 302:256-260 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(92)80454-o |
| Popis: | The tyrosine phenol lyase (EC 4.1.99.2) from Citrobacter intermedius has been crystallised in the apo form by vapour diffusion. The space group is P21212. The unit cell has dimensions a = 76.0 Å, b = 138.3 Å, c = 93.5 Å and it contains two subunits of the tetrameric molecule in the asymmetric unit, Diffraction data for the native enzyme and two heavy atom derivatives have been collected with synchrotron radiation and an image plate scanners. The structure has been solved at 2.7 Å resolution by isomorphous replacement with subsequent modification of the phases by averaging the density around the non-crystallographic symmetry axis. The electron density maps clearly show the relative orientation of the subunits and most of the trace of the polypeptide chain. Each subunit consists of two domains. The topology of the large domain appears to be similar to that of the aminotransferases. |
| Databáze: | OpenAIRE |
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