de.mpg.escidoc.pubman.appbase.FacesBean
English
 
Help Guide Disclaimer Contact us Login
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Crystal structure of KorA bound to operator DNA: insight into repressor cooperation in RP4 gene regulation

MPS-Authors

Lanka,  Erich
Max Planck Society;

Locator
There are no locators available
Fulltext (public)

1915.pdf
(Any fulltext), 8MB

Supplementary Material (public)
There is no public supplementary material available
Citation

König, B., Müller, J. J., Lanka, E., & Heinemann, U. (2009). Crystal structure of KorA bound to operator DNA: insight into repressor cooperation in RP4 gene regulation. Nucleic Acids Research, 37(6), 1915-1924. doi:10.1093/nar/gkp044.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-7E1C-D
Abstract
KorA is a global repressor in RP4 which regulates cooperatively the expression of plasmid genes whose products are involved in replication, conjugative transfer and stable inheritance. The structure of KorA bound to an 18-bp DNA duplex that contains the symmetric operator sequence and incorporates 5-bromo-deoxyuridine nucleosides has been determined by multiple-wavelength anomalous diffraction phasing at 1.96-Å resolution. KorA is present as a symmetric dimer and contacts DNA via a helix–turn–helix motif. Each half-site of the symmetric operator DNA binds one copy of the protein in the major groove. As confirmed by mutagenesis, recognition specificity is based on two KorA side chains forming hydrogen bonds to four bases within each operator half-site. KorA has a unique dimerization module shared by the RP4 proteins TrbA and KlcB. We propose that these proteins cooperate with the global RP4 repressor KorB in a similar manner via this dimerization module and thus regulate RP4 inheritance.