The X‐ray crystal structure of PA1607 from Pseudomonas aureginosa at 1.9 Å resolution—a putative transcription factor

Abstract

The structure of the PA1607 protein from Pseudomonas aureginosa was determined at 1.85 Å resolution using the Se‐Met multiwavelength anomalous diffraction (MAD) technique. PA1607 forms a dimer and adopts a winged‐helix motif similar to the MarR family of transcription regulators, though it has an unusual dimerization profile. The DNA‐binding regions and a putative metal‐binding site are not conserved in PA1607.