Structural highlights
Function
[CRP_ECOLI] This protein complexes with cyclic AMP and binds to specific DNA sites near the promoter to regulate the transcription of several catabolite-sensitive operons. The protein induces a severe bend in the DNA. Acts as a negative regulator of its own synthesis as well as for adenylate cyclase (cyaA), which generates cAMP.[1]
Publication Abstract from PubMed
The crystal structure of cyclic AMP-catabolite activator protein (CAP) from Escherichia coli containing cobalt(II) chloride and ammonium sulfate is reported at 1.97 A resolution. Each of the two CAP subunits in the asymmetric unit binds one cobalt(II) ion, in each case coordinated by N-terminal domain residues His19, His21 and Glu96 plus an additional acidic residue contributed via a crystal contact. The three identified N-terminal domain cobalt-binding residues are part of a region of CAP that is important for transcription activation at class II CAP-dependent promoters. Sulfate anions mediate additional crystal lattice contacts and occupy sites corresponding to DNA backbone phosphate positions in CAP-DNA complex structures.
Structure of catabolite activator protein with cobalt(II) and sulfate.,Rao RR, Lawson CL Acta Crystallogr F Struct Biol Commun. 2014 May;70(Pt 5):560-3. doi:, 10.1107/S2053230X14005366. Epub 2014 Apr 15. PMID:24817710[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Aiba H. Transcription of the Escherichia coli adenylate cyclase gene is negatively regulated by cAMP-cAMP receptor protein. J Biol Chem. 1985 Mar 10;260(5):3063-70. PMID:2982847
- ↑ Rao RR, Lawson CL. Structure of catabolite activator protein with cobalt(II) and sulfate. Acta Crystallogr F Struct Biol Commun. 2014 May;70(Pt 5):560-3. doi:, 10.1107/S2053230X14005366. Epub 2014 Apr 15. PMID:24817710 doi:http://dx.doi.org/10.1107/S2053230X14005366
