2iu6: Difference between revisions

Line 4:

==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==

Line 23:

[[Category: transferase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun~~ Feb ~~3 10~~:38:15 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:56:06 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==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==
@@ Line 23: / Line 23: @@
 [[Category: transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:38:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:56:06 2008''