Premium
The X‐ray crystal structure of PA1607 from Pseudomonas aureginosa at 1.9 Å resolution—a putative transcription factor
Author(s) -
Sieminska Edyta A.L.,
Xu Xiaohui,
Savchenko Alexei,
Sanders David A.R.
Publication year - 2007
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.062668207
Subject(s) - dimer , transcription factor , transcription (linguistics) , crystallography , binding site , crystal structure , biology , dna , chemistry , microbiology and biotechnology , genetics , stereochemistry , gene , linguistics , philosophy , organic chemistry
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.