Allosteric changes in the cAMP receptor protein of Escherichia coli: hinge reorientation.
The cAMP receptor protein (CRP) of Escherichia coli is a dimer of a two-domain subunit. It requires binding of cAMP for a conformational change in order to function as a site-specific DNA-binding protein that regulates gene activity. The hinge region connecting the cAMP-binding domain to the DNA-bin...
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| Published in: | Proc Natl Acad Sci U S A |
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| Main Authors: | , , |
| Format: | Artigo |
| Language: | Inglês |
| Published: |
National Academy of Sciences
1992
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| Subjects: | |
| Online Access: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC50200/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1409686/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.89.20.9700 |
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