English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
 Local TagsRelease HistoryDetailsSummary
  Crystal structure of KorA bound to operator DNA: insight into repressor cooperation in RP4 gene regulation

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.

Item is

 

show all hide all

Basic

show hide
Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0010-7E1C-D Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0010-7E1D-B
Genre: Journal Article
Alternative Title : NAR

Files

show Files
hide Files
:
1915.pdf (Any fulltext), 8MB
View   Save
File Permalink:
https://hdl.handle.net/11858/00-001M-0000-0010-7E1B-F
Name:
1915.pdf
Description:
-
OA-Status:
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
View
Copyright Date:
-
Copyright Info:
eDoc_access: PUBLIC
License:
-

Locators

show

Creators

show
hide
 Creators:
König, Bettina, Author
Müller, Jürgen J., Author
Lanka, Erich1, Author
Heinemann, Udo, Author
Affiliations:
1Max Planck Society, ou_persistent13              

Content

show
hide
Free keywords: -
 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.

Details

show
hide
Language(s): eng - English
 Dates: 2009-02-03
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 444333
URI: http://nar.oxfordjournals.org/cgi/reprint/37/6/1915?maxtoshow=&HITS=10&hits=10&RESULTFORMAT=1&andorexacttitle=and&andorexacttitleabs=and&andorexactfulltext=and&searchid=1&FIRSTINDEX=0&sortspec=relevance&volume=37&firstpage=1915&resourcetype=HWCIT
DOI: 10.1093/nar/gkp044
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Nucleic Acids Research
  Alternative Title : NAR
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 37 (6) Sequence Number: - Start / End Page: 1915 - 1924 Identifier: ISSN: 0305-1048