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2IU5

Dihydroxyacetone kinase operon activator DhaS

Summary for 2IU5
Entry DOI10.2210/pdb2iu5/pdb
DescriptorHTH-TYPE DHAKLM OPERON TRANSCRIPTIONAL ACTIVATOR DHAS (2 entities in total)
Functional Keywordstranscription, synthase, activator, tetr family
Biological sourceLACTOCOCCUS LACTIS SUBSP. LACTIS IL1403
Total number of polymer chains2
Total formula weight47149.61
Authors
Srinivas, A.,Christen, S.,Baumann, U.,Erni, B. (deposition date: 2006-05-27, release date: 2006-06-13, Last modification date: 2024-05-08)
Primary citationChristen, S.,Srinivas, A.,Bahler, P.,Zeller, A.,Pridmore, D.,Bieniossek, C.,Baumann, U.,Erni, B.
Regulation of the Dha Operon of Lactococcus Lactis: A Deviation from the Rule Followed by the Tetr Family of Transcription Regulators
J.Biol.Chem., 281:23129-, 2006
Cited by
PubMed Abstract: 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.
PubMed: 16760471
DOI: 10.1074/JBC.M603486200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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数据于2024-11-06公开中

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