2iu4: Difference between revisions

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[[Image:2iu4.gif|left|200px]]
{{Seed}}
[[Image:2iu4.png|left|200px]]


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{{STRUCTURE_2iu4|  PDB=2iu4  |  SCENE=  }}  
{{STRUCTURE_2iu4|  PDB=2iu4  |  SCENE=  }}  


'''DIHYDROXYACETONE KINASE OPERON CO-ACTIVATOR DHA-DHAQ'''
===DIHYDROXYACETONE KINASE OPERON CO-ACTIVATOR DHA-DHAQ===




==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.
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{{ABSTRACT_PUBMED_16760471}}


==About this Structure==
==About this Structure==
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[[Category: Lactococcus lacti]]
[[Category: Lactococcus lacti]]
[[Category: Transferase]]
[[Category: Transferase]]
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Revision as of 09:50, 28 July 2008

File:2iu4.png

Template:STRUCTURE 2iu4

DIHYDROXYACETONE KINASE OPERON CO-ACTIVATOR DHA-DHAQ

Template:ABSTRACT PUBMED 16760471

About this Structure

2IU4 is a Single protein structure of sequence from Lactococcus lactis. Full crystallographic information is available from OCA.

Reference

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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