|
|
| Line 1: |
Line 1: |
| [[Image:2iu6.gif|left|200px]] | | {{Seed}} |
| | [[Image:2iu6.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_2iu6| PDB=2iu6 | SCENE= }} | | {{STRUCTURE_2iu6| PDB=2iu6 | SCENE= }} |
|
| |
|
| '''REGULATION OF THE DHA OPERON OF LACTOCOCCUS LACTIS'''
| | ===REGULATION OF THE DHA OPERON OF LACTOCOCCUS LACTIS=== |
|
| |
|
|
| |
|
| ==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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16760471}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16760471 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_16760471}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| Line 30: |
Line 34: |
| [[Category: Kinase]] | | [[Category: Kinase]] |
| [[Category: Transferase]] | | [[Category: Transferase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:53:06 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:49:17 2008'' |
