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Structure of the transcription regulator CcpA from Lactococcus lactis

MPG-Autoren
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Loll,  Bernhard
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Zitation

Loll, B., Kowalczyk, M., Alings, C., Chieduch, A., Bardowski, J., Saenger, W., et al. (2007). Structure of the transcription regulator CcpA from Lactococcus lactis. Acta Crystallographica. Section D: Biological Crystallography (Copenhagen), 63, 431-436. doi:10.1107/S0907444907000546.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-002C-AB29-D
Zusammenfassung
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.