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pubmed-article:17322537pubmed:abstractTextThe structure of the PA1607 protein from Pseudomonas aureginosa was determined at 1.85 A 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.lld:pubmed
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pubmed-article:17322537pubmed:articleTitleThe X-ray crystal structure of PA1607 from Pseudomonas aureginosa at 1.9 A resolution--a putative transcription factor.lld:pubmed
pubmed-article:17322537pubmed:affiliationDepartment of Chemistry, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5C9, Canada.lld:pubmed
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