The polypeptide chain fold in tyrosine phenol‐lyase, a pyridoxal‐5′‐phosphate‐dependent enzyme

FEBS Letters

Dauter, Zbigniew²  Demidkina, Tatyana V.³  Vassylyev, Dmitry G.³  Antson, Alfred A.²  Wilson, Keith S.²  Murshudov, Garib N.¹  Harutyunyan, Emil H.¹  Terry, Howard²  Isupov, Michail N.¹  Strokopytov, Boris V.¹ 

[1] Institute of Crystallography, Russian Academy of Science, Leninsky pr. 59, Moscow 117333, Russia;European Molecular Biology Laboratory, DESY, Notkestrasse 85, D-2000 Hamburg 52, Germany;Engelhardt Institute of Molecular Biology, Russian Academy of Science, Vavilov str. 32, Moscow, 117984, Russia

关键词: Tyrosine phenol lyase;    X-ray analysis;    Polypeptide chain fold;    Bacterial;    pyridoxal-P;    pyridoxal-5′-phosphate;    AspAT;    aspartate aminotransferase;    TPL;    tyrosine phenol lyase;   

DOI  :  10.1016/0014-5793(92)80454-O

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown