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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Altenberg, Guillermo A. Cooper, Rebecca S. |
| Description | Author Affiliation: Cooper RS ( Department of Cell Physiology and Molecular Biophysics, and Center for Membrane Protein Research, Texas Tech Health Sciences Center, Lubbock, Texas 79430-6551 , USA.) |
| Abstract | In ATP-binding cassette proteins, the two nucleotide-binding domains (NBDs) work as dimers to bind and hydrolyze ATP, but the molecular mechanism of nucleotide hydrolysis is controversial. It is still unresolved whether hydrolysis leads to dissociation of the ATP-induced dimers or partial opening of the dimers such that the NBDs remain in contact during the hydrolysis cycle. We studied the bacterial lipid flippase MsbA by luminescence resonance energy transfer (LRET). The LRET signal between optical probes reacted with single-cysteine mutants was employed to follow NBD association/dissociation in real time. The intermonomer distances calculated from LRET data indicate that the NBDs separate completely following ATP hydrolysis, even in the presence of mm MgATP, and that the dissociation occurs following each hydrolysis cycle. The results support association/dissociation, as opposed to constant contact models, for the mode of operation of ATP-binding cassette proteins. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 29 |
| Volume Number | 288 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2013-07-19 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | ATP-Binding Cassette Transporters Chemistry Metabolism Bacterial Proteins Nucleotides Salmonella Typhimurium Adenosine Triphosphatases Biocatalysis Boron Compounds Energy Transfer Hydrolysis Kinetics Liposomes Luminescence Mutant Proteins Isolation & Purification Protein Binding Protein Structure, Tertiary Time Factors Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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