2hid
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REFINED NMR STRUCTURE OF PHOSPHOCARRIER HISTIDINE CONTAINING PROTEIN FROM BACILLUS SUBTILIS
OverviewOverview
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 alpha-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.
About this StructureAbout this Structure
2HID is a Single protein structure of sequence from Bacillus subtilis. This structure superseeds the now removed PDB entry 1HID. Full crystallographic information is available from OCA.
ReferenceReference
Phosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis., Jones BE, Rajagopal P, Klevit RE, Protein Sci. 1997 Oct;6(10):2107-19. PMID:9336834
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