Characterization of the Adenosine Triphosphatase Activity of the Periplasmic Histidine Permease, a Traffic ATPase (ABC Transporter)

Liu, Cheng Eureka; Liu, Peiqi; Ames, Giovanna Ferro‐Luzzi

doi:10.1074/jbc.272.35.21883

Cited by 116 publications

(138 citation statements)

References 46 publications

Supporting

Mentioning

120

Contrasting

Order By: Relevance

“…For CFTR, there is indirect evidence that ATP must bind to both sites to open the channel [59,60]. Finally, co-operative ATP binding suggests a role for two ATP molecules [50,[61][62][63][64]. However, it is possible to envisage an ABC transporter where one ATP is sufficient to stabilise the 'closed dimer' depending on the nature of the dimer interface.…”

Section: Stoichiometry Of Atp Binding and Hydrolysismentioning

confidence: 99%

“…It therefore seems that the conformational changes in the TMDs, at different steps in the catalytic cycle, may have different consequences for the different drug-binding sites for P-gp [68,69], TAP [70] and the histidine permease [71]. For some ABC transporters, the two pockets hydrolyse ATP non-simultaneously, for example, P-gp [22,52,63,72], MutS [36], and the bacterial histidine [50,61] and maltose [73] transporters. Consistent with this, the two nucleotidebinding pockets of a transporter frequently exhibit structural asymmetry even for HisP [29] and HlyB-NBD [40] where the two NBDs are identical in sequence.…”

Section: Stoichiometry Of Atp Binding and Hydrolysismentioning

confidence: 99%

See 1 more Smart Citation

Structure and function of ABC transporters: the ATP switch provides flexible control

Linton

Higgins

2006

Pflugers Arch - Eur J Physiol

189

157

View full text Add to dashboard Cite

ATP-binding cassette (ABC) transporters are ubiquitous integral membrane proteins that facilitate the transbilayer movement of ligands. They comprise, minimally, two transmembrane domains, which impart ligand specificity, and two nucleotide-binding domains (NBDs), which power the transport cycle. Almost 25 years of biochemistry is reviewed in light of the recent structure analyses resulting in the ATP-switch model for function in which the NBDs switch between a dimeric conformation, closed around two molecules of ATP, and a nucleotide-free, dimeric 'open' conformation. The flexibility of this switching mechanism has evolved to provide different kinetic control for different transporters and has also been co-opted to diverse functions other than transmembrane transport.

show abstract

Section: Stoichiometry Of Atp Binding and Hydrolysismentioning

confidence: 99%

Section: Stoichiometry Of Atp Binding and Hydrolysismentioning

confidence: 99%

Structure and function of ABC transporters: the ATP switch provides flexible control

Linton

Higgins

2006

Pflugers Arch - Eur J Physiol

189

157

View full text Add to dashboard Cite

show abstract

“…Biochemical analysis of the E. coli maltose ABC transporter 15 and the structure of the transporter complex BtuCD 16 established this head-to-tail arrangement as the archetype of the productive dimeric state of all ABC-ATPases. It explains the positive cooperativity in ATP hydrolysis that is observed for the ABC-ATPases in uptake systems, 17,18 and the negative effect of mutations in the ABC signature motif on ATP hydrolysis and transport activities. 5,6 Moreover, an association/dissociation cycle of the two ABCATPases, coupled to ATP binding and hydrolysis, could be part of a mechanism that explains the energy-transducing properties of ABC transporters.…”

Section: Introductionmentioning

confidence: 99%

Formation of the Productive ATP-Mg 2+ -bound Dimer of GlcV, an ABC-ATPase from Sulfolobus solfataricus

Verdon

Albers

Oosterwijk

et al. 2003

Journal of Molecular Biology

View full text Add to dashboard Cite

The ABC-ATPase GlcV from Sulfolobus solfataricus energizes an ABC transporter mediating glucose uptake. In ABC transporters, two ABC-ATPases are believed to form a head-to-tail dimer, with both monomers contributing conserved residues to each of the two productive active sites. In contrast, isolated GlcV, although active, behaves apparently as a monomer in the presence of ATP-Mg 2þ , AMPPNP-Mg 2þ or ATP alone. To resolve the oligomeric state of the active form of GlcV, we analysed the effects of changing the putative catalytic base, residue E166, into glutamine or alanine. Both mutants are, to different extents, defective in ATP hydrolysis, and gel-filtration experiments revealed their dimerization in the presence of ATP-Mg 2þ . Mutant E166Q forms dimers also in the presence of ATP alone, without Mg 2þ , whereas dimerization of mutant E166A requires both ATP and Mg 2þ . These results confirm earlier reports for other ABCATPases, but for the first time suggest the occurrence of a fast equilibrium between ATP-bound monomers and ATP-bound dimers. We further mutated two highly conserved residues of the ABC signature motif, S142 and G144, into alanine. The G144A mutant is completely inactive and fails to dimerize, indicating an essential role of this residue in stabilizing the productive dimeric state. Mutant S142A retained considerable activity, and was able to dimerize, thus implying that the interaction of the serine with ATP is not essential for dimerization and catalysis. Furthermore, although the E166A and G144A mutants each alone are inactive, they produce an active heterodimer, showing that disruption of one active site can be tolerated. Our data suggest that ABC-ATPases with partially degenerated catalytic machineries, as they occur in vivo, can still form productive dimers to drive transport.

show abstract

“…Assays typically contained 0.04 M MalFGK 2 and were initiated by addition of the proteoliposomes to other assay components preequilibrated at 37°C. The high Mg concentration used in this assay permeabilizes the proteoliposomes, allowing for assay of the MBP-stimulated ATPase activity of all transport complexes (22).…”

Section: Purification and Reconstitution Of The Maltose Transport Commentioning

confidence: 99%

Trapping the transition state of an ATP-binding cassette transporter: Evidence for a concerted mechanism of maltose transport

Chen¹

2001

Proceedings of the National Academy of Sciences

View full text Add to dashboard Cite

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 nucleotidebinding sites of the membrane transporter immediately after ATP hydrolysis, consistent with its ability to mimic the transition state of the ␥-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.A TP binding cassette (ABC) transporters are found in each of the phylogenetic kingdoms (1). ABC proteins have been identified that function in an increasing variety of uptake and efflux functions, including nutrient transport, protein and peptide transport, polysaccharide transport, and ion transport. Some ABC transporters function as multidrug efflux pumps in both prokaryotes and eukaryotes, and overexpression of the mammalian multidrug resistance protein MDR is sometimes responsible for multidrug resistance after chemotherapy in human cancer (2). Several human diseases have been traced to ABC proteins, including cystic fibrosis, hyperinsulinemia, and macular dystrophy (1, 3-5), making it important to understand their mechanism of action. The maltose transport system, one of at least 50 such systems in Escherichia coli (6), is well characterized both genetically and biochemically and provides an excellent model system for study of the ABC family (7). It consists of a periplasmic maltose-binding protein (MBP) and a multisubunit ABC transporter (MalFGK 2 ) containing two membrane integral subunits (MalF and MalG) and two copies of a peripheral subunit (MalK) that hydrolyzes ATP (7,8). MBP functions as the primary receptor for maltose, undergoing a conformational change to encapsulate the sugar and generate a high-affinity protein-ligand complex (9, 10). Maltose-loaded MBP then interacts with MalFGK 2 to stimulate ATP hydrolysis by MalK (11) and initiate the transport process. The mechanism by which MBP stimulates ATP hydrolysis is unknown, nor is it known how maltose is transferred from the high-affinity site in MBP to MalFGK 2 .We believe that many of these details can be elucidated by stabilizing and characterizing intermediates in the transport pathway. Vanadate, an analogue of inorganic phosphate, acts as a potent inhibitor of many ATPases, presumably because it can mimic the transition state for the ␥-phosphate of ATP during...

show abstract

Characterization of the Adenosine Triphosphatase Activity of the Periplasmic Histidine Permease, a Traffic ATPase (ABC Transporter)

Cited by 116 publications

References 46 publications

Structure and function of ABC transporters: the ATP switch provides flexible control

Structure and function of ABC transporters: the ATP switch provides flexible control

Formation of the Productive ATP-Mg 2+ -bound Dimer of GlcV, an ABC-ATPase from Sulfolobus solfataricus

Trapping the transition state of an ATP-binding cassette transporter: Evidence for a concerted mechanism of maltose transport

Contact Info

Product

Resources

About