2iu6: Difference between revisions

Revision as of 13:49, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2iu6.png

Template:STRUCTURE 2iu6

REGULATION OF THE DHA OPERON OF LACTOCOCCUS LACTISREGULATION OF THE DHA OPERON OF LACTOCOCCUS LACTIS

Template:ABSTRACT PUBMED 16760471

About this StructureAbout this Structure

2IU6 is a Single protein structure of sequence from Lactococcus lactis. 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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OCA

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-'''REGULATION OF THE DHA OPERON OF LACTOCOCCUS LACTIS'''
+===REGULATION OF THE DHA OPERON OF LACTOCOCCUS LACTIS===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16760471}}, adds the Publication Abstract to the page
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 [[Category: Kinase]]
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