2iu4: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 4: Line 4:


==Overview==
==Overview==
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.
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 Structure==
==About this Structure==
Line 26: Line 26:
[[Category: transferase]]
[[Category: transferase]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:38:14 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:56:00 2008''

Revision as of 18:56, 21 February 2008

File:2iu4.gif


2iu4, resolution 1.96Å

Drag the structure with the mouse to rotate

DIHYDROXYACETONE KINASE OPERON CO-ACTIVATOR DHA-DHAQ

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

2IU4 is a Single protein structure of sequence from Lactococcus lactis with and as ligands. 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

Page seeded by OCA on Thu Feb 21 17:56:00 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA