PMID:11171984: Difference between revisions

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<span style = 'font-size: large'> '''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</span>
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|{{TableHeadingColor}} |'''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.
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'''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
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!align=left  |Abstract
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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.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11171984 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC29290 PMC29290]
Online version:[http://dx.doi.org/10.1073/pnas.041542498 10.1073/pnas.041542498]
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|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11171984 PubMed]
!align=left  |Keywords
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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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Latest revision as of 04:14, 15 September 2013

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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