Crystallization and X-ray diffraction studies of the fatty-acid responsive transcription factor FadR from Escherichia coli.
FadR, an acylCoA-dependent Escherichia coli transcription factor controlling the expression of genes involved in fatty-acid degradation and synthesis, has been crystallized. Crystals of two binary complexes were obtained. The FadR-CoA complex crystallized in space group C222(1), with unit-cell parameters a = 61.3, b = 102.0, c = 91.3 A. The FadR-octanoyl-CoA complex crystallized in space group P6(5)22, with unit-cell parameters a = b = 59.7, c = 296.2 A. Both crystal forms diffracted to 3.5 A on a rotating-anode generator. In both crystal forms, the asymmetric unit contains one subunit. The protein is known to be a homodimer; each subunit consists of two domains of unknown fold. For the acyl-CoA-binding domain, a previously undetected sequence homology to PAS domains, in particular the photoactive yellow protein, is reported.
van Aalten
D M
DM
Biocenter Oulu and Department of Biochemistry, University of Oulu, Linnanmaa, FIN-90570 Oulu, Finland.
Knudsen
J
J
DiRusso
C C
CC
Kokko
T
T
Wierenga
R K
RK
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism*; D008969:Molecular Sequence Data; D020283:Photoreceptors, Microbial; D012097:Repressor Proteins / Q000737:chemistry* / Q000302:isolation & purification; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors / Q000737:chemistry* / Q000302:isolation & purification
D001426:Bacterial Proteins; C057119:FadR protein, Bacteria; D020283:Photoreceptors, Microbial; D012097:Repressor Proteins; D014157:Transcription Factors; C050162:photoactive yellow protein, Bacteria