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High resolution crystal structure of Sco5413, a widespread actinomycete MarR family transcriptional regulator of unknown function

DOI: 10.1002/prot.24197 DOI Help
PMID: 23042442 PMID Help

Authors: Tracey Holley (John Innes Centre) , Clare Stevenson (John Innes Centre) , M. Bibb (John Innes Centre, U.K.) , David Lawson (John Innes Centre)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Proteins: Structure, Function, And Bioinformatics

State: Published (Approved)
Published: November 2012

Abstract: The crystal structure of Sco5413 from Streptomyces coelicolor A3(2) has been determined at 1.25 Å resolution, the highest resolution reported for a MarR family transcriptional regulator. Putative orthologs are encoded by the majority of sequenced actinomycete genomes, and may play roles in regulating growth and antibiotic production, but they have yet to be assigned a precise function. Sco5413 forms a homodimer and, through comparisons with other MarR family protein structures, we postulate that it adopts a conformation compatible with DNA binding, and that a channel at the dimer interface, lined by well-conserved residues, is the binding site of an unidentified effector ligand.

Journal Keywords: protein–DNA interactions; protein–ligand interactions; winged helix fold; antibiotic biosynthesis; Streptomyces coelicolor

Diamond Keywords: Bacteria

Subject Areas: Biology and Bio-materials, Medicine

Instruments: I02-Macromolecular Crystallography , I24-Microfocus Macromolecular Crystallography

Added On: 09/11/2012 18:43

Discipline Tags:

Antibiotic Resistance Health & Wellbeing Structural biology Biophysics Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)