Back to Search
Start Over
Structure of catabolite activator protein with cobalt(II) and sulfate.
- Source :
-
Acta crystallographica. Section F, Structural biology communications [Acta Crystallogr F Struct Biol Commun] 2014 May; Vol. 70 (Pt 5), pp. 560-3. Date of Electronic Publication: 2014 Apr 15. - Publication Year :
- 2014
-
Abstract
- 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 Å 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.
Details
- Language :
- English
- ISSN :
- 2053-230X
- Volume :
- 70
- Issue :
- Pt 5
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section F, Structural biology communications
- Publication Type :
- Academic Journal
- Accession number :
- 24817710
- Full Text :
- https://doi.org/10.1107/S2053230X14005366