Artificial allosteric control of maltose binding protein.
We demonstrate the allosteric control of a protein based on mechanical tension. When substrate binding is accompanied by a significant change of conformation of the protein, a mechanical tension favoring one or the other conformation will alter the binding affinity for the substrate. We have constructed a chimera where the two lobes of the maltose-binding protein are covalently coupled to the ends of a DNA oligomer. The mechanical tension on the protein is controlled externally by exploiting the difference in stiffness between single stranded and double stranded DNA. We report that the binding affinity of the protein for its substrates is significantly altered by the tension.
Choi
Brian
B
Department of Physics and Astronomy, University of California-Los Angeles, Los Angeles, California 90095-1547, USA.
Zocchi
Giovanni
G
Canale
Stephen
S
Wu
Yim
Y
Chan
Sum
S
Perry
L Jeanne
LJ
D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D004247:DNA / Q000737:chemistry* / Q000648:ultrastructure*; D007536:Isomerism; D007700:Kinetics; D058619:Maltose-Binding Proteins; D011485:Protein Binding; D011487:Protein Conformation; D013314:Stress, Mechanical; D013329:Structure-Activity Relationship
D002352:Carrier Proteins; D058619:Maltose-Binding Proteins; D004247:DNA