Three‐dimensional structures of the central regulatory proteins of the bacterial phosphotransferase system, HPr and enzyme IIAglc
Open Access
- 1 January 1993
- journal article
- review article
- Published by Wiley in Journal of Cellular Biochemistry
- Vol. 51 (1) , 75-82
- https://doi.org/10.1002/jcb.240510114
Abstract
Enzyme IIA and HPr are central regulatory proteins of the bacterial phosphoenolpyruvate:sugar phosphotransferase (PTS) system. Three‐dimensional structures of the glucose enzyme IIA domain (IIAglc) and HPr of Bacillus subtilis and Escherichia coli have been studied by both X‐ray crystallography and Nuclear Magnetic Resonance (NMR) Spectroscopy. Phosphorylation of HPr of B. subtilis and IIAglc of E. coli have also been characterized by NMR spectroscopy. In addition, the binding interfaces of B. subtilis HPr and IIAglc have been identified from backbone chemical shift changes. This paper reviews these recent advances in the understanding of the three‐dimensional structures of HPr and IIAglc and their interaction with each other.Keywords
This publication has 35 references indexed in Scilit:
- Backbone dynamics of the Bacillus subtilis glucose permease IIA domain determined from nitrogen-15 NMR relaxation measurementsBiochemistry, 1992
- Three‐dimensional 15N‐1H‐1H and 15N‐13C‐1H nuclear‐magnetic resonance studies of HPr a central component of the phosphoenolpyruvate‐dependent phosphotransferase system from Escherichia coliEuropean Journal of Biochemistry, 1992
- Low resolution solution structure of the Bacillus subtilis glucose permease IIA domain derived from heteronuclear three‐dimensional NMR spectroscopyFEBS Letters, 1992
- Reexamination of the secondary and tertiary structure of histidine-containing protein from Escherichia coli by homonuclear and heteronuclear NMR spectroscopyBiochemistry, 1991
- Crystallization of the IIA domain of the glucose permease of Bacillus subtilisJournal of Molecular Biology, 1991
- Structure of the IIA domain of the glucose permease of Bacillus subtilis at 2.2-.ANG. resolutionBiochemistry, 1991
- Polypeptide backbone resonance assignments and secondary structure of Bacillus subtilis enzyme IIIglc determined by two-dimensional and three-dimensional heteronuclear NMR spectroscopyBiochemistry, 1991
- Sequence-specific proton NMR resonance assignments of Bacillus subtilus HPr: use of spectra obtained from mutants to resolve spectral overlapBiochemistry, 1990
- Structure and evolution of a multidomain multiphosphoryl transfer proteinJournal of Molecular Biology, 1990
- Two-dimensional proton NMR studies of histidine-containing protein from Escherichia coli. 1. Sequential resonance assignmentsBiochemistry, 1986