PMID:9309218

Citation	Tyrrell, R, Verschueren, KH, Dodson, EJ, Murshudov, GN, Addy, C and Wilkinson, AJ (1997) The structure of the cofactor-binding fragment of the LysR family member, CysB: a familiar fold with a surprising subunit arrangement. Structure 5:1017-32
Abstract	CysB is a tetrameric protein of identical subunits (M(r) = 36,000) which controls the expression of genes associated with the biosynthesis of cysteine in bacteria. CysB is both an activator and a repressor of transcription whose activity is responsive to the inducer N-acetylserine; thiosulphate and sulphide act as anti-inducers. CysB is a member of the LysR family of prokaryotic transcriptional regulatory proteins which share sequence similarities over approximately 280 residues including a putative helix-turn-helix DNA-binding motif at their N terminus. The aims of the present study were to explore further the complex molecular biology and curious ligand binding properties of CysB and to provide structural insights into the LysR family of proteins.
Links	PubMed
Keywords	Amino Acid Sequence; Bacterial Proteins/chemistry; Binding Sites; Crystallography, X-Ray; DNA-Binding Proteins/chemistry; Dimerization; Klebsiella pneumoniae/chemistry; Models, Molecular; Molecular Sequence Data; Molecular Weight; Peptide Fragments/chemistry; Protein Conformation; Sequence Alignment
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