Three-dimensional structures of the central regulatory proteins of the bacterial phosphotransferase system, HPr and enzyme IIAglc
✍ Scribed by Y. Chen; W. J. Fairbrother; P. E. Wright
- Publisher
- John Wiley and Sons
- Year
- 1993
- Tongue
- English
- Weight
- 766 KB
- Volume
- 51
- Category
- Article
- ISSN
- 0730-2312
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✦ Synopsis
Enzyme IIA and HPr are central regulatory proteins of the bacterial phosphoeno1pyruvate:sugar phosphotransferase (PTS) system. Three-dimensional structures of the glucose enzyme IIA domain (IIAgIC) and HPr of 5acillus 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 8. subtilis HPr and IIAg" 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 IIAg'c and their interaction with each other.