3Q5F
Crystal structure of the Salmonella transcriptional regulator SlyA in complex with DNA
Summary for 3Q5F
Entry DOI | 10.2210/pdb3q5f/pdb |
Related | 3QPT |
Descriptor | Transcriptional regulator slyA, DNA (5'-D(*AP*AP*TP*AP*AP*CP*TP*TP*AP*GP*CP*AP*AP*GP*CP*TP*AP*AP*TP*TP*AP*TP*A)-3'), DNA (5'-D(*TP*TP*AP*TP*AP*AP*TP*TP*AP*GP*CP*TP*TP*GP*CP*TP*AP*AP*GP*TP*TP*AP*T)-3') (3 entities in total) |
Functional Keywords | marr/slya protein family, winged helix-turn-helix, transcriptonal regulator, protein-dna complex, transcription-dna complex, transcription/dna |
Biological source | Salmonella enterica |
Total number of polymer chains | 4 |
Total formula weight | 47638.00 |
Authors | Dolan, K.T.,Duguid, E.M. (deposition date: 2010-12-28, release date: 2011-05-04, Last modification date: 2024-02-21) |
Primary citation | Dolan, K.T.,Duguid, E.M.,He, C. Crystal Structures of SlyA Protein, a Master Virulence Regulator of Salmonella, in Free and DNA-bound States. J.Biol.Chem., 286:22178-22185, 2011 Cited by PubMed Abstract: SlyA is a master virulence regulator that controls the transcription of numerous genes in Salmonella enterica. We present here crystal structures of SlyA by itself and bound to a high-affinity DNA operator sequence in the slyA gene. SlyA interacts with DNA through direct recognition of a guanine base by Arg-65, as well as interactions between conserved Arg-86 and the minor groove and a large network of non-base-specific contacts with the sugar phosphate backbone. Our structures, together with an unpublished structure of SlyA bound to the small molecule effector salicylate (Protein Data Bank code 3DEU), reveal that, unlike many other MarR family proteins, SlyA dissociates from DNA without large conformational changes when bound to this effector. We propose that SlyA and other MarR global regulators rely more on indirect readout of DNA sequence to exert control over many genes, in contrast to proteins (such as OhrR) that recognize a single operator. PubMed: 21550983DOI: 10.1074/jbc.M111.245258 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.96 Å) |
Structure validation
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