2p5k
Crystal structure of the N-terminal domain of AhrCCrystal structure of the N-terminal domain of AhrC
Structural highlights
FunctionARGR_BACSU Represses the synthesis of biosynthetic enzymes and activates the arginine catabolism. Controls the transcription of the two operons rocABC and rocDEF. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn Bacillus subtilis the concentration of L-arginine is controlled by the transcriptional regulator AhrC, which interacts with 18 bp DNA operator sites called ARG boxes in the promoters of arginine biosynthetic and catabolic operons. AhrC is a 100 kDa homohexamer, with each subunit having two domains. The C-terminal domains form the core, mediating intersubunit interactions and binding of the co-repressor L-arginine, whilst the N-terminal domains contain a winged helix-turn-helix DNA-binding motif and are arranged around the periphery. The N-terminal domain of AhrC has been expressed, purified and characterized and it has been shown that the fragment still binds DNA operators as a recombinant monomer. The DNA-binding domain has also been crystallized and the crystal structure refined to 1.0 A resolution is presented. A high-resolution structure of the DNA-binding domain of AhrC, the arginine repressor/activator protein from Bacillus subtilis.,Garnett JA, Baumberg S, Stockley PG, Phillips SE Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Nov 1;63(Pt, 11):914-7. Epub 2007 Oct 20. PMID:18007039[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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