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2Y7P

DntR Inducer Binding Domain in Complex with Salicylate. Trigonal crystal form

Summary for 2Y7P
Entry DOI10.2210/pdb2y7p/pdb
Related1UTB 1UTH 2Y7K 2Y7R 2Y7W 2Y84
DescriptorLYSR-TYPE REGULATORY PROTEIN, 2-HYDROXYBENZOIC ACID, 2,5,8,11,14,17,20,23,26,29,32,35,38,41,44,47,50,53,56,59,62,65,68,71,74,77,80-HEPTACOSAOXADOOCTACONTAN-82-OL, ... (4 entities in total)
Functional Keywordstranscription regulator, dna-binding, transcription, transcription factor, transcription regulation
Biological sourceBURKHOLDERIA SP.
Total number of polymer chains1
Total formula weight26349.55
Authors
Devesse, L.,Smirnova, I.,Lonneborg, R.,Kapp, U.,Brzezinski, P.,Leonard, G.A.,Dian, C. (deposition date: 2011-02-01, release date: 2011-07-20, Last modification date: 2024-05-01)
Primary citationDevesse, L.,Smirnova, I.,Lonneborg, R.,Kapp, U.,Brzezinski, P.,Leonard, G.A.,Dian, C.
Crystal Structures of Dntr Inducer Binding Domains in Complex with Salicylate Offer Insights Into the Activation of Lysr-Type Transcriptional Regulators.
Mol.Microbiol., 81:354-, 2011
Cited by
PubMed Abstract: Activation of LysR-type transcription factors (LTTRs) is thought to result from conformational changes that occur when inducer molecules bind to their Inducer Binding Domains (IBDs). However, the exact nature of these changes remains to be fully elucidated. We present the crystal structures of two truncated constructs of the LTTR DntR in their apo- forms and in complex with its natural inducer molecule, salicylate. These provide a fuller picture of the conformational changes that can occur in LTTR IBDs and offer insights that may be relevant when considering the mechanism of activation of LTTRs. Two of the crystal structures show that DntR IBDs can bind up to two inducer molecules. The full extent of conformational changes observed is achieved only when inducer molecules are bound in both binding sites identified. Point mutations disrupting the putative secondary binding site produce DntR variants with a reduced response to salicylate in a whole cell system, suggesting that this site is functionally relevant.
PubMed: 21692874
DOI: 10.1111/J.1365-2958.2011.07673.X
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.85 Å)
Structure validation

226707

數據於2024-10-30公開中

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