Structure of the Histidine-Containing Phosphocarrier Protein HPr from Bacillus subtilis at 2.0-Å Resolution

The crystal structure of the histidine-containing phosphocarrier protein (HPr) of the phosphoenolpyruvate:sugar phosphotransferase system (PTS) from Bacillus subtilis has been determined at 2.0-Å resolution and refined to a crystallographic residual error R-factor of 0.150. The secondary-structure f...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1992-03, Vol.89 (6), p.2499-2503
Hauptverfasser:	Herzberg, Osnat, Reddy, Prasad, Sutrina, Sarah, Saier, Milton H., Reizer, Jonathan, Kapadia, Geeta
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Atomic interactions Atoms Bacillus subtilis - metabolism Bacteria Bacterial Proteins - chemistry Binding Sites Biochemistry Cloning, Molecular Crystal structure Crystals Histidine Membrane transport proteins Models, Molecular Molecular Sequence Data Molecules Nitrogen Phosphoenolpyruvate Sugar Phosphotransferase System - chemistry Phosphoenolpyruvate Sugar Phosphotransferase System - isolation & purification Protein Conformation Proteins Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Salts Sugar Sulfates X-Ray Diffraction - methods
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