PMID:11171984
| Citation |
Chen, J, Sharma, S, Quiocho, FA and Davidson, AL (2001) Trapping the transition state of an ATP-binding cassette transporter: evidence for a concerted mechanism of maltose transport. Proc. Natl. Acad. Sci. U.S.A. 98:1525-30 |
|---|---|
| Abstract |
High-affinity uptake into bacterial cells is mediated by a large class of periplasmic binding protein-dependent transport systems, members of the ATP-binding cassette superfamily. In the maltose transport system of Escherichia coli, the periplasmic maltose-binding protein binds its substrate maltose with high affinity and, in addition, stimulates the ATPase activity of the membrane-associated transporter when maltose is present. Vanadate inhibits maltose transport by trapping ADP in one of the two nucleotide-binding sites of the membrane transporter immediately after ATP hydrolysis, consistent with its ability to mimic the transition state of the gamma-phosphate of ATP during hydrolysis. Here we report that the maltose-binding protein becomes tightly associated with the membrane transporter in the presence of vanadate and simultaneously loses its high affinity for maltose. These results suggest a general model explaining how ATP hydrolysis is coupled to substrate transport in which a binding protein stimulates the ATPase activity of its cognate transporter by stabilizing the transition state. |
| Links |
PubMed PMC29290 Online version:10.1073/pnas.041542498 |
| Keywords |
ATP-Binding Cassette Transporters/antagonists & inhibitors; ATP-Binding Cassette Transporters/metabolism; Adenosine Diphosphate/metabolism; Adenosine Triphosphatases/antagonists & inhibitors; Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Bacterial Proteins/antagonists & inhibitors; Bacterial Proteins/metabolism; Biological Transport; Carrier Proteins/metabolism; Escherichia coli Proteins; Maltose/metabolism; Maltose-Binding Proteins; Membrane Proteins/antagonists & inhibitors; Membrane Proteins/metabolism; Monosaccharide Transport Proteins; Periplasmic Binding Proteins; Vanadates/pharmacology |
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