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Publication Abstract from PubMed

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 A resolution in the absence of cognate DNA. The phases were derived by molecular replacement and the structure was refined to crystallographic R and R(free) 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.

Structure of the transcription regulator CcpA from Lactococcus lactis.,Loll B, Kowalczyk M, Alings C, Chieduch A, Bardowski J, Saenger W, Biesiadka J Acta Crystallogr D Biol Crystallogr. 2007 Apr;63(Pt 4):431-6. Epub 2007, Mar 16. PMID:17372346^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.