3qpt

Publication Abstract from PubMed

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 R65, as well as interactions between conserved R86 and the minor groove and a large network of non-base-specific contacts to the sugar-phosphate backbone. Our structures, together with an unpublished structure of SlyA bound to the drug salicylate (PDB: 3DEU), reveal that unlike many other MarR-family proteins, SlyA dissociates from DNA without large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 in order to exert control over many genes, in contrast to proteins such as OhrR which recognize a single operator.

Crystal structures of SlyA, a master virulence regulator of Salmonella, in free and DNA-bound states.,Dolan KT, Duguid EM, He C J Biol Chem. 2011 May 5. PMID:21550983^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.