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Structure of catabolite activator protein with cobalt(II) and sulfate.

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.

SUBMITTER: Rao RR

PROVIDER: S-EPMC4014319 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature

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Structure of catabolite activator protein with cobalt(II) and sulfate.

Rao Ramya R RR Lawson Catherine L CL

Acta crystallographica. Section F, Structural biology communications 20140415 Pt 5

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 ...[more]

PMID: 24817710

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