Premium
Structure of catabolite activator protein with cobalt(II) and sulfate
Author(s) -
Rao Ramya R.,
Lawson Catherine L.
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14005366
Subject(s) - catabolite repression , activator (genetics) , cobalt , crystal structure , chemistry , ammonium sulfate , residue (chemistry) , promoter , escherichia coli , binding site , crystallography , biochemistry , stereochemistry , inorganic chemistry , gene , organic chemistry , gene expression , mutant
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.