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Both maltose-binding protein and ATP are required for nucleotide-binding domain closure in the intact maltose ABC transporter
The maltose transporter MalFGK(2) of Escherichia coli is a member of the ATP-binding cassette superfamily. A periplasmic maltose-binding protein (MBP) delivers maltose to MalFGK(2) and stimulates its ATPase activity. Site-directed spin labeling EPR spectroscopy was used to study the opening and clos...
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| Hoofdauteurs: | , , , , |
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| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
National Academy of Sciences
2008
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2529024/ https://ncbi.nlm.nih.gov/pubmed/18725638 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0803799105 |
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