5AE4
Structures of inactive and activated DntR provide conclusive evidence for the mechanism of action of LysR transcription factors
Summary for 5AE4
Entry DOI | 10.2210/pdb5ae4/pdb |
Related | 5AE5 |
Descriptor | LYSR-TYPE REGULATORY PROTEIN, THIOCYANATE ION (2 entities in total) |
Functional Keywords | transcription, lysr-type transcription regulators, lttr, transcription factor, helix-turn-helix, dna binding protein, rossmann-like fold, autoinducing mutant, h169t-dntr |
Biological source | BURKHOLDERIA CEPACIA |
Total number of polymer chains | 2 |
Total formula weight | 69786.65 |
Authors | Lerche, M.,Dian, C.,Round, A.,Lonneborg, R.,Brzezinski, P.,Leonard, G.A. (deposition date: 2015-08-25, release date: 2016-01-13, Last modification date: 2024-01-10) |
Primary citation | Lerche, M.,Dian, C.,Round, A.,Lonneborg, R.,Brzezinski, P.,Leonard, G.A. The Solution Configurations of Inactive and Activated Dntr Have Implications for the Sliding Dimer Mechanism of Lysr Transcription Factors. Sci.Rep., 6:19988-, 2016 Cited by PubMed: 26817994DOI: 10.1038/SREP19988 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.3 Å) |
Structure validation
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