2O20
Crystal structure of transcription regulator CcpA of Lactococcus lactis
Summary for 2O20
Entry DOI | 10.2210/pdb2o20/pdb |
Related | 1RZR 1SHI 1SXG 1SXH 2FEP 2HSG |
Descriptor | Catabolite control protein A, SULFATE ION, CHLORIDE ION, ... (4 entities in total) |
Functional Keywords | ccpa, transcriptional regulator, helix-turn-helix, transcription |
Biological source | Lactococcus lactis |
Total number of polymer chains | 8 |
Total formula weight | 293944.86 |
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 citation | Loll, 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: 17372346DOI: 10.1107/S0907444907000546 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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