PMID:10739923
| Citation |
van Aalten, DM, Knudsen, J, DiRusso, CC, Kokko, T and Wierenga, RK (2000) Crystallization and X-ray diffraction studies of the fatty-acid responsive transcription factor FadR from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 56:469-71 |
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| Abstract |
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. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/isolation & purification; Crystallization; Crystallography, X-Ray; Escherichia coli/metabolism; Molecular Sequence Data; Photoreceptors, Microbial; Repressor Proteins/chemistry; Repressor Proteins/isolation & purification; Sequence Alignment; Sequence Homology, Amino Acid; Transcription Factors/chemistry; Transcription Factors/isolation & purification |
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