2HSG

Structure of transcription regulator CcpA in its DNA-free state

Summary for 2HSG

• Entry DOI: 10.2210/pdb2hsg/pdb
• Related: 1RZR 1SHI 1SXG 1SXH 1ZVV 2FEP
• Descriptor: Glucose-resistance amylase regulator (1 entity in total)
• Functional Keywords: ccpa, transcriptional regulator, transcription regulator
• Biological source: Bacillus megaterium
• Total number of polymer chains: 1
• Total formula weight: 36685.65

Authors

Loll, B.,Alings, C.,Saenger, W.,Biesiadka, J. (deposition date: 2006-07-21, release date: 2007-06-05, Last modification date: 2023-08-30)

Primary citation

Loll, B.,Saenger, W.,Biesiadka, J.
Structure of full-length transcription regulator CcpA in the apo form.
Biochim.Biophys.Acta, 1774:732-736, 2007

PubMed Abstract: The catabolite control protein A (CcpA) from Bacillus megaterium is a member of the bacterial repressor protein family GalR-LacI. CcpA functions as master transcriptional regulator of carbon catabolite repression/regulation in firmicutes. Here we present the crystal structure of full-length apo CcpA at 2.5 A resolution from B. megaterium. The structure reveals the location of the helix-turn-helix domain as well as the hinge region, which were not visible due to their high flexibility in earlier crystallographic studies on CcpA molecules. The structure of the apo CcpA homodimer in the present form is in contrast to other reported structures for CcpA.

PubMed: 17500051
DOI: 10.1016/j.bbapap.2007.03.020

Experimental method

X-RAY DIFFRACTION (2.5 Å)