Structure of the transcription regulator CcpA from Lactococcus lactis.
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.
Loll
Bernhard
B
Institute for Chemistry and Biochemistry/Crystallography, Freie Universität Berlin, Takustrasse 6, D-14195 Berlin, Germany.
Kowalczyk
Magdalena
M
Alings
Claudia
C
Chieduch
André
A
Bardowski
Jacek
J
Saenger
Wolfram
W
Biesiadka
Jacek
J
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D013294:Lactococcus lactis / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D017510:Protein Folding; D012097:Repressor Proteins / Q000737:chemistry* / Q000378:metabolism; D014158:Transcription, Genetic
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D012097:Repressor Proteins; C069286:catabolite control proteins, bacteria