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Papers In Press, published online ahead of print April 25, 2003
Laboratory of Chemical Physics, NIDDK, National Institutes of Health, Bethesda, MD 20892-0510
Corresponding Author: mariusc{at}intra.niddk.nih.gov
The solution structure of the final phosphoryl transfer complex in the glucose-specific arm of the Escherichia coli phosphotransferase system (PTS), between enzyme IIAGlucose (IIAGlc) and the cytoplasmic B domain (IIBGlc) of the glucose transporter IICBGlc, has been solved by NMR. The interface (~1200 Å2 buried surface) is formed by the interaction of a concave depression on IIAGlc with a convex protrusion on IIBGlc. The phosphoryl donor and acceptor residues, His90 of IIAGlc and Cys35 of IIBGlc, are in close proximity and buried at the center of the interface. Cys35 is primed for nucleophilic attack on the phosphorus atom by stabilization of the thiolate anion (pKa ~ 6.5) through intramolecular hydrogen bonding interactions with several adjacent backbone amide groups. Hydrophobic intermolecular contacts are supplemented by peripheral electrostatic interactions involving an alternating distribution of positively and negatively charged residues on the interaction surfaces of both proteins. Salt bridges between the Asp38/Asp94 pair of IIAGlc and the Arg38/Arg40 pair of IIBGlc neutralize the accumulation of negative charge in the vicinity of both the Sg atom of Cys35 and the phosphoryl group in the complex. A pentacoordinate phosphoryl transition state is readily accomodated without any change in backbone conformation, and the structure of the complex accounts for the preferred directionality of phosphoryl transfer between IIAGlc and IIBGlc. The structures of IIAGlc-IIBGlc and the two upstream complexes of the glucose PTS (EI-HPr and IIAGlc-HPr) reveal a cascade in which highly overlapping binding sites on HPr and IIAGlc recognize structurally diverse proteins.
J. Biol. Chem, 10.1074/jbc.M302677200
Submitted on March 17, 2003
Revised on April 25, 2003
Accepted on April 25, 2003
Solution structure of the phosphoryl transfer complex between the signal transducing protein IIAglucose and the cytoplasmic domain of the glucose transporter IICBglucose of the Escherichia coli glucose phosphotransferase system
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