1jem: Difference between revisions

Revision as of 20:07, 1 July 2008

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File:1jem.png

Template:STRUCTURE 1jem

NMR STRUCTURE OF HISTIDINE PHOSPHORYLATED FORM OF THE PHOSPHOCARRIER HISTIDINE CONTAINING PROTEIN FROM BACILLUS SUBTILIS, NMR, 25 STRUCTURESNMR STRUCTURE OF HISTIDINE PHOSPHORYLATED FORM OF THE PHOSPHOCARRIER HISTIDINE CONTAINING PROTEIN FROM BACILLUS SUBTILIS, NMR, 25 STRUCTURES

Template:ABSTRACT PUBMED 9336834

About this StructureAbout this Structure

1JEM is a Single protein structure of sequence from Bacillus subtilis. Full experimental 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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OCA

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-'''NMR STRUCTURE OF HISTIDINE PHOSPHORYLATED FORM OF THE PHOSPHOCARRIER HISTIDINE CONTAINING PROTEIN FROM BACILLUS SUBTILIS, NMR, 25 STRUCTURES'''
+===NMR STRUCTURE OF HISTIDINE PHOSPHORYLATED FORM OF THE PHOSPHOCARRIER HISTIDINE CONTAINING PROTEIN FROM BACILLUS SUBTILIS, NMR, 25 STRUCTURES===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9336834}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9336834 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9336834}}
 ==About this Structure==
-JEM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JEM OCA].
+JEM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JEM OCA].
 ==Reference==
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 [[Category: Phosphohistidine]]
 [[Category: Pt]]
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