The Response Regulator OmpR Oligomerizes via β-Sheets to Form Head-to-head Dimers
- 29 July 2005
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 350 (5) , 843-856
- https://doi.org/10.1016/j.jmb.2005.05.057
Abstract
No abstract availableKeywords
This publication has 51 references indexed in Scilit:
- Three-dimensional crystal structure of the transcription factor PhoB receiver domainJournal of Molecular Biology, 1999
- Structural relationships in the OmpR family of winged-helix transcription factorsJournal of Molecular Biology, 1997
- The DNA-binding domain of OmpR: crystal structures of a winged helix transcription factorStructure, 1997
- Escherichia coli positive regulator OmpR has a large loop structure at the putative RNA polymerase interaction siteNature Structural & Molecular Biology, 1997
- Identification of a phosphorylation site and functional analysis of conserved aspartic acid residues of OmpR, a transcriptional activator for ompF and ompC in Escherichia coliMolecular Microbiology, 1993
- Crystal structure of Escherichia coli CheY refined at 1.7-A resolutionJournal of Biological Chemistry, 1991
- Location of phosphorylation site and DNA‐binding site of a positive regulator, OmpR, involved in activation of the osmoregulatory genes of Escherichia coliFEBS Letters, 1989
- Three-dimensional structure of CheY, the response regulator of bacterial chemotaxisNature, 1989
- Location of DNA‐binding segment of a positive regulator, OmpR, involved in activation of the ompF and ompC genes of Escherichia coliFEBS Letters, 1988
- Genetic analysis of the ompB locus in Escherichia coli K-12Journal of Molecular Biology, 1981