Crystallization and preliminary X-ray analysis of UMP/CMP-kinase from Dictyostelium discoideum with the specific bisubstrate inhibitor P1-(adenosine 5')-P5-(uridine 5')-pentaphosphate (UP5A)

FEBS Lett. 1995 Apr 17;363(1-2):22-4. doi: 10.1016/0014-5793(95)00271-a.

Abstract

UMP/CMP-kinase (UK) from the slime mold Dictyostelium discoideum has been purified to high homogeneity and co-crystallized with the bisubstrate inhibitor P1-(adenosine 5')-P5-(uridine 5')-pentaphosphate (UP5A). UP5A binds to UK with a dissociation constant (Kd) of 3 +/- 0.5 nM at 25 degrees C and pH 7.5. This is some 50-fold tighter than the binding of P1,P5-(diadenosine 5')-pentaphosphate (AP5A, Kd = 160 +/- 15 nM). AP5A is a bisubstrate inhibitor that is specific for adenylate kinase. The crystals have the symmetry of the tetragonal space group P4(1)2(1)2 or its enantiomorph P4(3)2(1)2. The unit cell dimensions are a = b = 78.5 A and c = 101.4 A. The crystals diffract to a Bragg spacing of 2.1 A.

Publication types

  • Comparative Study

MeSH terms

  • Animals
  • Binding Sites
  • Chemical Phenomena
  • Chemistry, Physical
  • Crystallization
  • Crystallography, X-Ray*
  • Dictyostelium / enzymology*
  • Dinucleoside Phosphates / chemistry*
  • Dinucleoside Phosphates / metabolism
  • Dithioerythritol / pharmacology
  • Hydrogen-Ion Concentration
  • Nucleoside-Phosphate Kinase / antagonists & inhibitors
  • Nucleoside-Phosphate Kinase / chemistry*
  • Nucleoside-Phosphate Kinase / metabolism
  • Spectrometry, Fluorescence

Substances

  • Dinucleoside Phosphates
  • P(1)-(adenosine-5')-P(5)-(uridine-5')pentaphosphate
  • P(1),P(5)-di(adenosine-5'-)pentaphosphate
  • Dithioerythritol
  • cytidylate kinase
  • Nucleoside-Phosphate Kinase