Binding of the Catabolite Repressor Protein CcpA to Its DNA Target Is Regulated by Phosphorylation of its Corepressor HPr
Open Access
- 1 October 1997
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 272 (42), 26530-26535
- https://doi.org/10.1074/jbc.272.42.26530
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- Cooperative and non-cooperative DNA binding modes of catabolite control protein CcpA from Bacillus megaterium result from sensing two different signalsJournal of Molecular Biology, 1997
- The Domain Organization of Human Topoisomerase IJournal of Biological Chemistry, 1996
- Phosphorylation of serine‐46 in HPr, a key regulatory protein in bacteria, results in stabilization of its solution structureProtein Science, 1995
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995
- Specific recognition of the Bacillus subtilis gnt cis‐acting catabolite‐responsive element by a protein complex formed between CcpA and seryl‐phosphorylated HPrMolecular Microbiology, 1995
- High-resolution Structure of the Phosphorylated Form of the Histidine-containing Phosphocarrier Protein HPr fromEscherichia coliDetermined by Restrained Molecular Dynamics from NMR-NOE DataJournal of Molecular Biology, 1995
- Possible function and some properties of the CcpA protein of Bacillus subtilisMicrobiology, 1994
- The NMR determination of the IIAmtl binding site on HPr of the Escherichia coli phosphoenol pyruvate‐dependent phosphotransferase systemFEBS Letters, 1993
- The MIDAS display systemJournal of Molecular Graphics, 1988
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970