Acta Cryst. (2007). D63, 431-436 [ doi:10.1107/S0907444907000546 ]
Abstract: Catabolite control protein A (CcpA) functions as master transcriptional regulator of carbon catabolism in Firmicutes. It belongs to the family of bacterial repressor/regulator proteins. Here, the crystal structure of the 76 kDa homodimeric CcpA protein from Lactococcus lactis subsp. lactis IL1403 is presented at 1.9 Å resolution in the absence of cognate DNA. The phases were derived by molecular replacement and the structure was refined to crystallographic R and Rfree factors of 0.177 and 0.211, respectively. The presence of a sulfate molecule in the direct vicinity of a putative effector-binding site in the monomer allowed the derivation of a model for the possible binding of small organic effector molecules.
PDB reference: 2o20
Keywords: DNA-binding protein/regulation; MALDI-TOF mass spectrometry.
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