NDLI: Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-A resolution.

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Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-A resolution.

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Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-A resolution.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Herzberg, O. Reddy, P. Saier, M. H. Sutrina, S. Kapadia, G. Reizer, J.
Description	Author Affiliation: Herzberg O ( Maryland Biotechnology Institute, University of Maryland, Rockville.);
Abstract	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-A resolution and refined to a crystallographic residual error R-factor of 0.150. The secondary-structure folding topology of the molecule is that of an open-face beta-sandwich formed by four antiparallel beta-strands packed against three alpha-helices. The active-site histidine, His-15, caps the N terminus of the first helix, suggesting that the helix dipole plays a role in stabilizing the phosphorylated state of the histidine. A sulfate anion located between His-15 and the neighboring Arg-17 has been identified in the electron-density map. Association of this negatively charged species with the two key catalytic residues implies that the crystal structure resembles the phosphorylated state of the protein. A model of the phosphorylated form of the molecule is proposed, in which the negatively charged phosphoryl group interacts with two main-chain nitrogen atoms of the following helix and with the guanidinium group of Arg-17. It is also proposed that the phosphoryl transfer from HPr to the IIA domain of the glucose permease involves Arg-17 switching between two salt bridges: one with the phosphorylated histidyl of HPr and the other with two aspartyl residues associated with the active site of the IIA domain of glucose permease, which are accessible upon complex formation.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	6
Volume Number	89
Language	English
Publisher	National Academy of Sciences
Publisher Date	1992-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacillus Subtilis Metabolism Histidine Phosphoenolpyruvate Sugar Phosphotransferase System Chemistry Amino Acid Sequence Bacterial Proteins Binding Sites Cloning, Molecular Models, Molecular Molecular Sequence Data Isolation & Purification Protein Conformation Recombinant Proteins X-Ray Diffraction Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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