2iu6
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REGULATION OF THE DHA OPERON OF LACTOCOCCUS LACTIS
OverviewOverview
Dihydroxyacetone (Dha) kinases are a novel family of kinases with, signaling and metabolic functions. Here we report the x-ray structures of, the transcriptional activator DhaS and the coactivator DhaQ and, characterize their function. DhaQ is a paralog of the Dha binding Dha, kinase subunit; DhaS belongs to the family of TetR repressors although, unlike all known members of this family, it is a transcriptional, activator. DhaQ and DhaS form a stable complex that in the presence of Dha, activates transcription of the Lactococcus lactis dha operon. Dha, covalently binds to DhaQ through a hemiaminal bond with a histidine and, thereby induces a conformational change, which is propagated to the, surface via a cantilever-like structure. DhaS binding protects an inverted, repeat whose sequence is GGACACATN6ATTTGTCC and renders two GC base pairs, of the operator DNA hypersensitive to DNase I cleavage. The proximal, half-site of the inverted repeat partially overlaps with the predicted -35, consensus sequence of the dha promoter.
About this StructureAbout this Structure
2IU6 is a Single protein structure of sequence from Lactococcus lactis with as ligand. Active as Glucokinase, with EC number 2.7.1.2 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Regulation of the Dha operon of Lactococcus lactis: a deviation from the rule followed by the Tetr family of transcription regulators., Christen S, Srinivas A, Bahler P, Zeller A, Pridmore D, Bieniossek C, Baumann U, Erni B, J Biol Chem. 2006 Aug 11;281(32):23129-37. Epub 2006 Jun 7. PMID:16760471
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