2iu4: Difference between revisions
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== Structural highlights == | == 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> | [[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>[[Ligand|Ligands:]]</b> <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | ||
<b>[[Non-Standard_Residue|NonStd Res:]]</b> <scene name='pdbligand=HIQ:1-[1,2-DIHYDROXY-1-(HYDROXYMETHYL)ETHYL]-L-HISTIDINE'>HIQ</scene><br> | |||
<b>[[Related_structure|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> | <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> | ||
<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iu4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2iu4 RCSB], [http://www.ebi.ac.uk/pdbsum/2iu4 PDBsum]</span><br> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|right]] | [[Image:Consurf_key_small.gif|right]] | ||
Revision as of 13:11, 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. Ligands: 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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