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5AE4

Structures of inactive and activated DntR provide conclusive evidence for the mechanism of action of LysR transcription factors

Summary for 5AE4
Entry DOI10.2210/pdb5ae4/pdb
Related5AE5
DescriptorLYSR-TYPE REGULATORY PROTEIN, THIOCYANATE ION (2 entities in total)
Functional Keywordstranscription, lysr-type transcription regulators, lttr, transcription factor, helix-turn-helix, dna binding protein, rossmann-like fold, autoinducing mutant, h169t-dntr
Biological sourceBURKHOLDERIA CEPACIA
Total number of polymer chains2
Total formula weight69786.65
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 citationLerche, 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: 26817994
DOI: 10.1038/SREP19988
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.3 Å)
Structure validation

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