2iu5
From Proteopedia
(New page: 200px<br /><applet load="2iu5" size="450" color="white" frame="true" align="right" spinBox="true" caption="2iu5, resolution 1.60Å" /> '''DIHYDROXYACETONE KIN...) |
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| - | [[Image:2iu5.gif|left|200px]]<br /><applet load="2iu5" size=" | + | [[Image:2iu5.gif|left|200px]]<br /><applet load="2iu5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2iu5, resolution 1.60Å" /> | caption="2iu5, resolution 1.60Å" /> | ||
'''DIHYDROXYACETONE KINASE OPERON ACTIVATOR DHAS'''<br /> | '''DIHYDROXYACETONE KINASE OPERON ACTIVATOR DHAS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Dihydroxyacetone (Dha) kinases are a novel family of kinases with | + | 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== | ||
| - | 2IU5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis_subsp._lactis_il1403 Lactococcus lactis subsp. lactis il1403]. Full crystallographic information is available from [http:// | + | 2IU5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis_subsp._lactis_il1403 Lactococcus lactis subsp. lactis il1403]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IU5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tetr family]] | [[Category: tetr family]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:56:03 2008'' |
Revision as of 15:56, 21 February 2008
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DIHYDROXYACETONE KINASE OPERON ACTIVATOR DHAS
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.
About this Structure
2IU5 is a Single protein structure of sequence from Lactococcus lactis subsp. lactis il1403. 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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