Crystallization and preliminary X-ray analysis of 4-coumarate:CoA ligase from Arabidopsis thaliana

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Mar 1;67(Pt 3):409-11. doi: 10.1107/S1744309111002181. Epub 2011 Feb 25.

Abstract

4-Coumarate:CoA ligase 2 (4CL2) from Arabidopsis thaliana catalyzes the ATP-dependent formation of the 4-coumaroyl-CoA thioester through the formation of 4-coumarate-AMP. Recombinant 4CL2 protein was expressed in Escherichia coli and crystallized by the sitting-drop vapour-diffusion method. The crystals belonged to space group P2(1), with unit-cell parameters a=91.6, b=55.5, c=124.4 Å, α=γ=90.0, β=111.1°.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyl Coenzyme A / chemistry
  • Acyl Coenzyme A / metabolism
  • Arabidopsis / enzymology*
  • Arabidopsis Proteins / chemistry*
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism
  • Coenzyme A Ligases / chemistry*
  • Coenzyme A Ligases / genetics
  • Coenzyme A Ligases / metabolism
  • Crystallization
  • Crystallography, X-Ray
  • Molecular Sequence Data
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism

Substances

  • Acyl Coenzyme A
  • Arabidopsis Proteins
  • Recombinant Proteins
  • 4-coumaroyl-coenzyme A
  • Coenzyme A Ligases
  • 4-coumarate-CoA ligase