2o20

Crystal structure of transcription regulator CcpA of Lactococcus lactis

spinqualitylabelsall models 2o20, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2o20 is a 8 chain structure with sequence from Lactococcus lactis. Full crystallographic information is available from OCA. Ligands: CL, SO4 Related: 1rzr, 1sxg, 1sxh, 1shi, 2fep, 2hsg Gene: ccpa (Lactococcus lactis) Activity: Glucokinase, with EC number 2.7.1.2 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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