- Crp domain
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Crp 
crystal structure of the e.coli crp-camp complex Identifiers Symbol Crp Pfam PF00325 Pfam clan CL0123 InterPro IPR001808 PROSITE PDOC00041 SCOP 1cgp Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary 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]
References
- ^ 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. 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.
This article includes text from the public domain Pfam and InterPro IPR001808
Categories:- Protein domains
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