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

Academic Article

Abstract

  • 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. © 1992.
  • Published In

  • FEBS Letters  Journal
  • Digital Object Identifier (doi)

    Author List

  • Antson AA; Strokopytov BV; Murshudov GN; Isupov MN; Harutyunyan EH; Demidkina TV; Vassylyev DG; Dauter Z; Terry H; Wilson KS
  • Start Page

  • 256
  • End Page

  • 260
  • Volume

  • 302
  • Issue

  • 3