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2O20

Crystal structure of transcription regulator CcpA of Lactococcus lactis

Summary for 2O20
Entry DOI10.2210/pdb2o20/pdb
Related1RZR 1SHI 1SXG 1SXH 2FEP 2HSG
DescriptorCatabolite control protein A, SULFATE ION, CHLORIDE ION, ... (4 entities in total)
Functional Keywordsccpa, transcriptional regulator, helix-turn-helix, transcription
Biological sourceLactococcus lactis
Total number of polymer chains8
Total formula weight293944.86
Authors
Loll, B.,Kowalczyk, M.,Alings, C.,Chieduch, A.,Bardowski, J.,Saenger, W.,Biesiadka, J. (deposition date: 2006-11-29, release date: 2007-03-27, Last modification date: 2023-08-30)
Primary citationLoll, B.,Kowalczyk, M.,Alings, C.,Chieduch, A.,Bardowski, J.,Saenger, W.,Biesiadka, J.
Structure of the transcription regulator CcpA from Lactococcus lactis
Acta Crystallogr.,Sect.D, 63:431-436, 2007
Cited by
PubMed 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.
PubMed: 17372346
DOI: 10.1107/S0907444907000546
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

238895

數據於2025-07-16公開中

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