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The polypeptide chain fold in tyrosine phenol‐lyase, a pyridoxal‐5′‐phosphate‐dependent enzyme
Author(s) -
Antson Alfred A.,
Strokopytov Boris V.,
Murshudov Garib N.,
Isupov Michail N.,
Harutyunyan Emil H.,
Demidkina Tatyana V.,
Vassylyev Dmitry G.,
Dauter Zbigniew,
Terry Howard,
Wilson Keith S.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80454-o
Subject(s) - crystallography , chemistry , molecule , pyridoxal phosphate , stereochemistry , protein subunit , enzyme , cofactor , biochemistry , organic chemistry , gene
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 P2 1 2 1 2. 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.