Using neutron protein crystallography to understand enzyme mechanisms.
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.
Fox Chase Cancer Center, 333 Cottman Avenue, Philadelphia, PA 19111-2497, USA.
Jenny P
JP
Glusker
H L
HL
Carrell
Andrey Y
AY
Kovalevsky
Leif
L
Hanson
S Zoe
SZ
Fisher
Marat
M
Mustyakimov
Sax
S
Mason
Trevor
T
Forsyth
Paul
P
Langan
D019747:Aldose-Ketose Isomerases / Q000737:chemistry* / Q000378:metabolism*; D002384:Catalysis; D017666:Deuterium Oxide / Q000378:metabolism; D006859:Hydrogen; D008670:Metals / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D033363:Neutron Diffraction; D009502:Neutrons; D011487:Protein Conformation; D011522:Protons; D014996:Xylulose / Q000378:metabolism*
D008670:Metals; D011522:Protons; D014996:Xylulose; D006859:Hydrogen; D019747:Aldose-Ketose Isomerases; C023298:xylose isomerase; D017666:Deuterium Oxide