4FT8
E. coli Catabolite Activator Protein with Cobalt and Sulfate Ligands
Summary for 4FT8
| Entry DOI | 10.2210/pdb4ft8/pdb |
| Descriptor | Catabolite gene activator, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | winged helix-turn-helix, dna binding protein, cobalt binding, sulfate binding, transcription activator |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 49107.58 |
| Authors | Rao, R.,Lawson, C.L. (deposition date: 2012-06-27, release date: 2013-12-18, Last modification date: 2023-09-13) |
| Primary citation | Rao, R.R.,Lawson, C.L. Structure of catabolite activator protein with cobalt(II) and sulfate. Acta Crystallogr F Struct Biol Commun, 70:560-563, 2014 Cited by PubMed 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. PubMed: 24817710DOI: 10.1107/S2053230X14005366 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.966 Å) |
Structure validation
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