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Protein Science (2007), 16:543-549. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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PROTEIN STRUCTURE REPORT

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

Edyta A.L. Sieminska1, Xiaohui Xu2, Alexei Savchenko2, and David A.R. Sanders1

1 Department of Chemistry, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5C9, Canada
2 Ontario Center for Structural Proteomics, University Health Network, Toronto, Ontario M5G 2C4, Canada

(RECEIVED November 17, 2006; FINAL REVISION December 11, 2006; ACCEPTED December 12, 2006)

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.

Keywords: transcription factor; winged-helix; crystal structure


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