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Phosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis
Author(s) -
Jones Bryan E.,
Rajagopal Ponni,
Klevit Rachel E.
Publication year - 1997
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560061006
Subject(s) - pep group translocation , bacillus subtilis , histidine , phosphorylation , chemistry , biochemistry , stereochemistry , phosphoenolpyruvate carboxykinase , phosphotransferase , enzyme , escherichia coli , biology , bacteria , gene , genetics
The histidine‐containing protein (HPr) of bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS) serves a central role in a series of phosphotransfer reactions used for the translocation of sugars across cell membranes. These studies report the high‐definition solution structures of both the unphosphorylated and histidine phosphorylated (P‐His) forms of HPr from Bacillus subtilis. Consistent with previous NMR studies, local conformational adjustments occur upon phosphorylation of His 15, which positions the phosphate group to serve as a hydrogen bond acceptor for the amide protons of Ala 16 and Arg 17 and to interact favorably with the α‐helix macrodipole. However, the positively charged side chain of the highly conserved Arg 17 does not appear to interact directly with phospho‐His 15, suggesting that Arg 17 plays a role in the recognition of other PTS enzymes or in phosphotransfer reactions directly. Unlike the results reported for Escherichia coli P‐His HPr (Van Nuland NA, Boelens R, Scheek RM, Robillard GT, 1995, J Mol Biol 246:180‐193), our data indicate that phosphorylation of His 15 is not accompanied by adoption of unfavorable backbone conformations for active site residues in B. subtilis P‐Ser HPr.