2hid: Difference between revisions
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'''REFINED NMR STRUCTURE OF PHOSPHOCARRIER HISTIDINE CONTAINING PROTEIN FROM BACILLUS SUBTILIS''' | {{Structure | ||
|PDB= 2hid |SIZE=350|CAPTION= <scene name='initialview01'>2hid</scene> | |||
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|LIGAND= | |||
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'''REFINED NMR STRUCTURE OF PHOSPHOCARRIER HISTIDINE CONTAINING PROTEIN FROM BACILLUS SUBTILIS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2HID is a [ | 2HID is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. This structure supersedes the now removed PDB entry 1HID. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HID OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9336834 9336834] | ||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: histidine containing protein]] | [[Category: histidine containing protein]] | ||
[[Category: phosphotransferase]] | [[Category: phosphotransferase]] | ||
[[Category: | [[Category: pt]] | ||
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Revision as of 18:17, 20 March 2008
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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 supersedes 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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