cAMP receptor protein
From Wikipedia, the free encyclopedia
 |
|
| Structure of the E. coli Cyclic AMP Receptor Protein. | |
| Identifiers | |
|---|---|
| Symbol | CRP |
| Alt. symbols | CAP |
| Entrez | 947867 |
| PDB | 1I5Z |
| RefSeq | NP_417816.1 |
| UniProt | P0ACJ8 |
| Other data | |
cAMP receptor protein (in short CRP, also known as catabolite gene activator protein (in short CAP)) is a regulatory protein in bacteria. This protein binds cAMP, which causes a conformational change that allows the protein to bind tightly to a specific DNA sequence in the promoters of the genes it controls.[1] The genes regulated by this protein are mostly involved in energy metabolism, such as galactose, citrate, or the PEP group translocation system.[2][3]
[edit] References
- ^ Harman JG (2001). "Allosteric regulation of the cAMP receptor protein". Biochim. Biophys. Acta 1547 (1): 1–17. doi:10.1016/S0167-4838(01)00187-X. PMID 11343786.
- ^ Weickert MJ, Adhya S (1993). "The galactose regulon of Escherichia coli". Mol. Microbiol. 10 (2): 245–51. doi:10.1111/j.1365-2958.1993.tb01950.x. PMID 7934815.
- ^ Bott M (1997). "Anaerobic citrate metabolism and its regulation in enterobacteria". Arch. Microbiol. 167 (2–3): 78–88. doi:10.1007/s002030050419. PMID 9133329.
[edit] External links
 |
This bacteria-related article is a stub. You can help Wikipedia by expanding it. |
 |
This protein-related article is a stub. You can help Wikipedia by expanding it. |
