In molecular biology, the CAT RNA-binding domain (Co-AntiTerminator RNA-binding domain) is a protein domain found at the amino terminus of a family of transcriptional antiterminator proteins. This domain forms a dimer in the crystal structure.[1] Transcriptional antiterminators of the BglG/SacY family are regulatory proteins that mediate the induction of sugar metabolizing operons in Gram-positive and Gram-negative bacteria. Upon activation, these proteins bind to specific targets in nascent mRNAs, thereby preventing abortive dissociation of the RNA polymerase from the DNA template.[2]
| CAT_RBD | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 structure of the lict bacterial antiterminator protein in complex with its rna target | |||||||||
| Identifiers | |||||||||
| Symbol | CAT_RBD | ||||||||
| Pfam | PF03123 | ||||||||
| InterPro | IPR004341 | ||||||||
| SCOP2 | 1h99 / SCOPe / SUPFAM | ||||||||
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References
edit- ^ van Tilbeurgh H, Manival X, Aymerich S, Lhoste JM, Dumas C, Kochoyan M (August 1997). "Crystal structure of a new RNA-binding domain from the antiterminator protein SacY of Bacillus subtilis". EMBO J. 16 (16): 5030–6. doi:10.1093/emboj/16.16.5030. PMC 1170137. PMID 9305644.
- ^ Declerck N, Vincent F, Hoh F, Aymerich S, van Tilbeurgh H (November 1999). "RNA recognition by transcriptional antiterminators of the BglG/SacY family: functional and structural comparison of the CAT domain from SacY and LicT". J. Mol. Biol. 294 (2): 389–402. doi:10.1006/jmbi.1999.3256. PMID 10610766.