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The dimeric form of the unphosphorylated response regulator BaeR
Author(s) -
Choudhury Hassanul G.,
Beis Konstantinos
Publication year - 2013
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 - 10.1002/pro.2311
Subject(s) - dimer , phosphorylation , effector , response regulator , chemistry , kinase , biology , escherichia coli , biophysics , microbiology and biotechnology , biochemistry , gene , bacterial protein , organic chemistry
Bacterial response regulators (RRs) can regulate the expression of genes that confer antibiotic resistance; they contain a receiver and an effector domain and their ability to bind DNA is based on the dimerization state. This is triggered by phosphorylation of the receiver domain by a kinase. However, even in the absence of phosphorylation RRs can exist in equilibrium between monomers and dimers with phosphorylation shifting the equilibrium toward the dimer form. We have determined the crystal structure of the unphosphorylated dimeric BaeR from Escherichia coli . The dimer interface is formed by a domain swap at the receiver domain. In comparison with the unphosphorylated dimeric PhoP from Mycobacterium tuberculosis , BaeR displays an asymmetry of the effector domains.