Diamond Publications - Search Results

Search Again...

These results include publications that have not yet been reviewed and processed by Diamond Light Source. To view only processed publications click here.

You can use the folder icon under Actions to collate papers as required. You can then click on View Folder in the left-hand navigation to review and/or download your folder.

One item found (0 items not approved).

Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography	Structural insights into the DNA recognition mechanism by the bacterial transcription factor PdxR Ida Freda , Cécile Exertier , Anna Barile , Antonio Chaves-Sanjuan , Mirella Vivoli Vega , Misha N. Isupov , Nicholas J. Harmer , Elena Gugole , Paolo Swuec , Martino Bolognesi , Anita Scipioni , Carmelinda Savino , Martino luigi Di salvo , Roberto Contestabile , Beatrice Vallone , Angela Tramonti , Linda Celeste Montemiglio Nucleic Acids Research 33 DOI: 10.1093/nar/gkad552 Diamond Proposal Number(s): [11945] Open Access Show Abstract ▼ Abstract: Specificity in protein–DNA recognition arises from the synergy of several factors that stem from the structural and chemical signatures encoded within the targeted DNA molecule. Here, we deciphered the nature of the interactions driving DNA recognition and binding by the bacterial transcription factor PdxR, a member of the MocR family responsible for the regulation of pyridoxal 5′-phosphate (PLP) biosynthesis. Single particle cryo-EM performed on the PLP-PdxR bound to its target DNA enabled the isolation of three conformers of the complex, which may be considered as snapshots of the binding process. Moreover, the resolution of an apo-PdxR crystallographic structure provided a detailed description of the transition of the effector domain to the holo-PdxR form triggered by the binding of the PLP effector molecule. Binding analyses of mutated DNA sequences using both wild type and PdxR variants revealed a central role of electrostatic interactions and of the intrinsic asymmetric bending of the DNA in allosterically guiding the holo-PdxR–DNA recognition process, from the first encounter through the fully bound state. Our results detail the structure and dynamics of the PdxR–DNA complex, clarifying the mechanism governing the DNA-binding mode of the holo-PdxR and the regulation features of the MocR family of transcription factors.	Jun 2023

Instruments / Technical Area

Publication Details

Published

Actions

I03-Macromolecular Crystallography

Structural insights into the DNA recognition mechanism by the bacterial transcription factor PdxR