Using neutron protein crystallography to understand enzyme mechanisms

Acta Crystallogr D Biol Crystallogr. 2010 Nov;66(Pt 11):1257-61. doi: 10.1107/S0907444910027915. Epub 2010 Oct 20.

Abstract

A description is given of the results of neutron diffraction studies of the structures of four different metal-ion complexes of deuterated D-xylose isomerase. These represent four stages in the progression of the biochemical catalytic action of this enzyme. Analyses of the structural changes observed between the various three-dimensional structures lead to some insight into the mechanism of action of this enzyme.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Aldose-Ketose Isomerases / chemistry*
  • Aldose-Ketose Isomerases / metabolism*
  • Catalysis
  • Deuterium Oxide / metabolism
  • Hydrogen
  • Metals / chemistry
  • Metals / metabolism*
  • Models, Molecular
  • Neutron Diffraction*
  • Neutrons*
  • Protein Conformation
  • Protons
  • Xylulose / metabolism*

Substances

  • Metals
  • Protons
  • Xylulose
  • Hydrogen
  • Aldose-Ketose Isomerases
  • xylose isomerase
  • Deuterium Oxide