The 1.9 Å resolution structure of phospho-serine 46 HPr from Enterococcus faecalis
- 3 November 2000
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 303 (4), 545-553
- https://doi.org/10.1006/jmbi.2000.4166
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- The hprK gene of Enterococcus faecalis encodes a novel bifunctional enzyme: the HPr kinase/phosphataseMolecular Microbiology, 1999
- PRD — a protein domain involved in PTS‐dependent induction and carbon catabolite repression of catabolic operons in bacteriaMolecular Microbiology, 1998
- A novel protein kinase that controls carbon catabolite repression in bacteriaMolecular Microbiology, 1998
- New protein kinase and protein phosphatase families mediate signal transduction in bacterial catabolite repressionProceedings of the National Academy of Sciences, 1998
- Binding of the Catabolite Repressor Protein CcpA to Its DNA Target Is Regulated by Phosphorylation of its Corepressor HPrJournal of Biological Chemistry, 1997
- Protein kinase‐dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in Gram‐positive bacteriaMolecular Microbiology, 1995
- Enzymes II of the phospho enol pyruvate-dependent phosphotransferase systems: Their structure and function in carbohydrate transportBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1994
- Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteriaMicrobiological Reviews, 1993
- THE BACTERIAL PHOSPHOENOL-PYRUVATE: GLYCOSE PHOSPHOTRANSFERASE SYSTEMAnnual Review of Biochemistry, 1990
- Bacterial phosphoenolpyruvate-dependent phosphotransferase system: P-Ser-HPr and its possible regulatory functionBiochemistry, 1984