Saturation transfer difference NMR reveals functionally essential kinetic differences for a sugar-binding repressor protein.
The binding kinetics of disaccharides trehalose and trehalose-6-phosphate to repressor protein TreR have been determined using STD NMR and shed light on the contrasting biological roles of these two sugars.
Department of Chemistry, University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford, UK OX1 3TA.
Ignacio
I
Pérez-Victoria
Sebastian
S
Kemper
Mitul K
MK
Patel
John M
JM
Edwards
James C
JC
Errey
Lucia F
LF
Primavesi
Matthew J
MJ
Paul
Timothy D W
TD
Claridge
Benjamin G
BG
Davis
D001665:Binding Sites; D003198:Computer Simulation; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D011485:Protein Binding; D012097:Repressor Proteins / Q000737:chemistry* / Q000378:metabolism; D013403:Sugar Phosphates / Q000737:chemistry*; D014199:Trehalose / Q000031:analogs & derivatives* / Q000737:chemistry*
D029968:Escherichia coli Proteins; D012097:Repressor Proteins; D013403:Sugar Phosphates; C490609:TreR protein, E coli; C082722:trehalose-6-phosphate; D014199:Trehalose