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Studies of the Maltose Transport System Reveal a Mechanism for Coupling ATP Hydrolysis to Substrate Translocation without Direct Recognition of Substrate
The ATPase activity of the maltose transporter (MalFGK(2)) is dependent on interactions with the maltose-binding protein (MBP). To determine whether direct interactions between the translocated sugar and MalFGK(2) are important for the regulation of ATP hydrolysis, we used an MBP mutant (sMBP) that...
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| Main Authors: | , |
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| Format: | Artigo |
| Language: | Inglês |
| Published: |
American Society for Biochemistry and Molecular Biology
2010
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| Subjects: | |
| Online Access: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2857007/ https://ncbi.nlm.nih.gov/pubmed/20147285 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.089078 |
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