Crystal structure of transketolase in complex with thiamine thiazolone diphosphate, an analogue of the reaction intermediate, at 2.3 A resolution.
The crystal structure of the complex of transketolase and thiamine thiazolone diphosphate has been determined at 2.3 A resolution. The complex has a structure which closely resembles that of this enzyme with the cofactor ThDP. This is consistent with the observation that the binding of the analogue to transketolase involves ground state rather than transition state interactions. Since thiamine thiazolone diphosphate resembles an expected intermediate in the catalytic pathway, the structure of the intermediate was modelled from the crystal structure. Based on this model, enzymic groups responsible for binding of the intermediate and proton transfer during catalysis are suggested.
Nilsson
U
U
Department of Molecular Biology, Swedish University of Agricultural Sciences, Biomedical Center, Uppsala.
Lindqvist
Y
Y
Kluger
R
R
Schneider
G
G
D001665:Binding Sites; D003460:Crystallization; D003461:Crystallography; D006860:Hydrogen Bonding; D008958:Models, Molecular; D015394:Molecular Structure; D011485:Protein Binding; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013835:Thiamine Pyrophosphate / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D014174:Transketolase / Q000737:chemistry* / Q000378:metabolism
C014222:thiamine thiazolone pyrophosphate; D014174:Transketolase; D013835:Thiamine Pyrophosphate