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Updated: Jul 16, 2026

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Published on: July 21, 2014
Structure of the transcription regulator CcpA from Lactococcus lactis
Bernhard Loll1, Magdalena Kowalczyk, Claudia Alings
1Institute for Chemistry and Biochemistry/Crystallography, Freie Universität Berlin, Takustrasse 6, D-14195 Berlin, Germany.
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 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.
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