2iu4: Difference between revisions
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[[Image: | ==DIHYDROXYACETONE KINASE OPERON CO-ACTIVATOR DHA-DHAQ== | ||
<StructureSection load='2iu4' size='340' side='right' caption='[[2iu4]], [[Resolution|resolution]] 1.96Å' scene=''> | |||
== Structural highlights == | |||
[[2iu4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IU4 OCA]. <br> | |||
<b>Related:</b> [[2iu6|2iu6]]<br> | |||
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iu/2iu4_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:16760471</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
[[Category: Glucokinase]] | [[Category: Glucokinase]] | ||
[[Category: Lactococcus lactis]] | [[Category: Lactococcus lactis]] | ||
Revision as of 11:32, 30 April 2014
DIHYDROXYACETONE KINASE OPERON CO-ACTIVATOR DHA-DHAQDIHYDROXYACETONE KINASE OPERON CO-ACTIVATOR DHA-DHAQ
Structural highlights2iu4 is a 2 chain structure with sequence from Lactococcus lactis. Full crystallographic information is available from OCA. Related: 2iu6 Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDihydroxyacetone (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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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