English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
 Local TagsRelease HistoryDetailsSummary
  An Src Homology 3-like Domain Is Responsible for Dimerization of the Repressor Protein KorB Encoded by the Promiscuous IncP Plasmid RP4

Delbrück, H., Ziegelin, G., Lanka, E., & Heinemann, U. (2002). An Src Homology 3-like Domain Is Responsible for Dimerization of the Repressor Protein KorB Encoded by the Promiscuous IncP Plasmid RP4. Journal of Biological Chemistry, 277(6), 4191-4198.

Item is

 

show all hide all

Basic

show hide
Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0010-8C58-5 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0010-8C59-3
Genre: Journal Article
Alternative Title : J Biol Chem

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Delbrück, Heinrich, Author
Ziegelin, Günter1, Author
Lanka, Erich1, Author
Heinemann, Udo, Author
Deutsche Forschungsgemeinschaft Grants SFB 344, GRK 80/2,3, and He 1318/24 and the Fonds der Chemischen Industrie, Editor  
Affiliations:
1Max Planck Society, ou_persistent13              

Content

show
hide
Free keywords: -
 Abstract: KorB is a regulatory protein encoded by the conjugative plasmid RP4 and a member of the ParB family of bacterial partitioning proteins. The protein regulates the expression of plasmid genes whose products are involved in replication, transfer, and stable inheritance of RP4 by binding to palindromic 13-bp DNA sequences (5'-TTTAGC(G/C)GCTAAA-3') present 12 times in the 60-kb plasmid. Here we report the crystal structure of KorB-C, the C-terminal domain of KorB comprising residues 297-358. The structure of KorB-C was solved in two crystal forms. Quite unexpectedly, we find that KorB-C shows a fold closely resembling the Src homology 3 (SH3) domain, a fold well known from proteins involved in eukaryotic signal transduction. From the arrangement of molecules in the asymmetric unit, it is concluded that two molecules form a functionally relevant dimer. The detailed analysis of the dimer interface and a chemical cross-linking study suggest that the C-terminal domain is responsible for stabilizing the dimeric form of KorB in solution to facilitate binding to the palindromic operator sequence. The KorB-C crystal structure extends the range of protein-protein interactions known to be promoted by SH3 and SH3-like domains.

Details

show
hide
Language(s): eng - English
 Dates: 2002-02-01
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 24573
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Biological Chemistry
  Alternative Title : J Biol Chem
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 277 (6) Sequence Number: - Start / End Page: 4191 - 4198 Identifier: -