2JCG

Apo form of the catabolite control protein A (ccpA) from bacillus megaterium, with the DNA binding domain

Summary for 2JCG

• Entry DOI: 10.2210/pdb2jcg/pdb
• Related: 1RZR 1SXG 1SXH 1SXI 1ZVV
• Descriptor: GLUCOSE-RESISTANCE AMYLASE REGULATOR, CALCIUM ION (3 entities in total)
• Functional Keywords: megaterium, dna-binding, transcription, ccpa, bacillus, apo- form, activator, repressor, transcription regulation, catabolite control protein a
• Biological source: BACILLUS MEGATERIUM
• Total number of polymer chains: 1
• Total formula weight: 36711.70

Authors

Singh, R.K.,Panjikar, S.,Palm, G.J.,Hinrichs, W. (deposition date: 2006-12-22, release date: 2007-03-06, Last modification date: 2023-12-13)

Primary citation

Singh, R.K.,Palm, G.J.,Panjikar, S.,Hinrichs, W.
Structure of the Apo Form of the Catabolite Control Protein a (Ccpa) from Bacillus Megaterium with a DNA-Binding Domain.
Acta Crystallogr.,Sect.F, 63:253-, 2007

PubMed Abstract: Crystal structure determination of catabolite control protein A (CcpA) at 2.6 A resolution reveals for the first time the structure of a full-length apo-form LacI-GalR family repressor protein. In the crystal structures of these transcription regulators, the three-helix bundle of the DNA-binding domain has only been observed in cognate DNA complexes; it has not been observed in other crystal structures owing to its mobility. In the crystal packing of apo-CcpA, the protein-protein contacts between the N-terminal three-helix bundle and the core domain consisted of interactions between the homodimers that were similar to those between the corepressor protein HPr and the CcpA N-subdomain in the ternary DNA complex. In contrast to the DNA complex, the apo-CcpA structure reveals large subdomain movements in the core, resulting in a complete loss of contacts between the N-subdomains of the homodimer.

PubMed: 17401189
DOI: 10.1107/S1744309107008949

Experimental method

X-RAY DIFFRACTION (2.6 Å)