1AL3

COFACTOR BINDING FRAGMENT OF CYSB FROM KLEBSIELLA AEROGENES

Summary for 1AL3

• Entry DOI: 10.2210/pdb1al3/pdb
• Descriptor: CYS REGULON TRANSCRIPTIONAL ACTIVATOR CYSB, SULFATE ION (3 entities in total)
• Functional Keywords: lysr family, cysteine biosynthesis, transcription regulation
• Biological source: Klebsiella aerogenes
• Cellular location: Cytoplasm: P45600
• Total number of polymer chains: 1
• Total formula weight: 36104.17

Authors

Verschueren, K.H.G.,Tyrrell, R.,Wilkinson, A.J. (deposition date: 1997-06-10, release date: 1997-12-24, Last modification date: 2024-02-07)

Primary citation

Tyrrell, R.,Verschueren, K.H.,Dodson, E.J.,Murshudov, G.N.,Addy, C.,Wilkinson, A.J.
The structure of the cofactor-binding fragment of the LysR family member, CysB: a familiar fold with a surprising subunit arrangement.
Structure, 5:1017-1032, 1997

PubMed 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.

PubMed: 9309218
DOI: 10.1016/S0969-2126(97)00254-2

Experimental method

X-RAY DIFFRACTION (1.8 Å)