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.
Pérez-Victoria
Ignacio
I
Department of Chemistry, University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford, UK OX1 3TA.
Kemper
Sebastian
S
Patel
Mitul K
MK
Edwards
John M
JM
Errey
James C
JC
Primavesi
Lucia F
LF
Paul
Matthew J
MJ
Claridge
Timothy D W
TD
Davis
Benjamin G
BG
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