In molecular biology, the CRP domain is a protein domain consisting of a helix-turn-helix (HTH) motif. It is found at the C-terminus of numerous bacterial transcription regulatory proteins. These proteins bind DNA via the CRP domain. These proteins are very diverse, but for convenience may be grouped into subfamilies on the basis of sequence similarity. This family groups together a range of proteins, including ANR, CRP, CLP, CysR, FixK, Flp, FNR, FnrN, HlyX and NtcA.[1][2]
| Crp | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of the e.coli crp-camp complex | |||||||||
| Identifiers | |||||||||
| Symbol | Crp | ||||||||
| Pfam | PF00325 | ||||||||
| Pfam clan | CL0123 | ||||||||
| InterPro | IPR001808 | ||||||||
| PROSITE | PDOC00041 | ||||||||
| SCOP2 | 1cgp / SCOPe / SUPFAM | ||||||||
| CDD | cd00092 | ||||||||
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References edit
- ^ Korner H, Sofia HJ, Zumft WG (December 2003). "Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: exploiting the metabolic spectrum by controlling alternative gene programs". FEMS Microbiol. Rev. 27 (5): 559–92. doi:10.1016/s0168-6445(03)00066-4. PMID 14638413.
- ^ Busby S, Ebright RH (October 1999). "Transcription activation by catabolite activator protein (CAP)". J. Mol. Biol. 293 (2): 199–213. doi:10.1006/jmbi.1999.3161. PMID 10550204.