The dimeric form of the unphosphorylated response regulator BaeR

Choudhury, Hassanul G. and Beis, Konstantino (2013) The dimeric form of the unphosphorylated response regulator BaeR. Protein Science, 22 9: 1287-1293. doi:10.1002/pro.2311

Author Choudhury, Hassanul G.
Beis, Konstantino
Title The dimeric form of the unphosphorylated response regulator BaeR
Journal name Protein Science   Check publisher's open access policy
ISSN 0961-8368
Publication date 2013
Year available 2013
Sub-type Article (original research)
DOI 10.1002/pro.2311
Open Access Status
Volume 22
Issue 9
Start page 1287
End page 1293
Total pages 7
Place of publication Hoboken, NJ United States
Publisher Wiley-Blackwell Publishing, Inc.
Language eng
Subject 1303 Specialist Studies in Education
1312 Molecular Biology
Abstract 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.
Keyword Asymmetric dimer
Domain swap receiver domain
Effector domain
Unphosphorylated response regulator
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
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