TY - JOUR
T1 - Crystallization and X-ray diffraction studies of the fatty-acid responsive transcription factor FadR from Escherichia coli
AU - Van Aalten, Daan M.F.
AU - Knudsen, Jens
AU - DiRusso, Concetta C.
AU - Kokko, Tanja
AU - Wierenga, Rik K.
PY - 2000
Y1 - 2000
N2 - 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 C2221, with unit-cell parameters a = 61.3, b = 102.0, c = 91.3 Å. The FadR-octanoyl-CoA complex crystallized in space group P6522, with unit-cell parameters a = b = 59.7, c = 296.2 Å. Both crystal forms diffracted to 3.5 Å 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.
AB - 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 C2221, with unit-cell parameters a = 61.3, b = 102.0, c = 91.3 Å. The FadR-octanoyl-CoA complex crystallized in space group P6522, with unit-cell parameters a = b = 59.7, c = 296.2 Å. Both crystal forms diffracted to 3.5 Å 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.
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U2 - 10.1107/S0907444900000937
DO - 10.1107/S0907444900000937
M3 - Article
C2 - 10739923
AN - SCOPUS:0034095982
SN - 0907-4449
VL - 56
SP - 469
EP - 471
JO - Acta Crystallographica Section D: Biological Crystallography
JF - Acta Crystallographica Section D: Biological Crystallography
IS - 4
ER -