1jem: Difference between revisions

Revision as of 14:21, 21 February 2008

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

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

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

Page seeded by OCA on Thu Feb 21 13:21:45 2008

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OCA

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-[[Image:1jem.jpg|left|200px]]<br /><applet load="1jem" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1jem.jpg|left|200px]]<br /><applet load="1jem" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1jem" />
 '''NMR STRUCTURE OF HISTIDINE PHOSPHORYLATED FORM OF THE PHOSPHOCARRIER HISTIDINE CONTAINING PROTEIN FROM BACILLUS SUBTILIS, NMR, 25 STRUCTURES'''<br />
 ==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 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 Structure==
-JEM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JEM OCA].
+JEM is a [http://en.wikipedia.org/wiki/Single_protein 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].
 ==Reference==
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 [[Category: Bacillus subtilis]]
 [[Category: Single protein]]
-[[Category: Jones, B.E.]]
+[[Category: Jones, B E.]]
-[[Category: Klevit, R.E.]]
+[[Category: Klevit, R E.]]
 [[Category: Rajagopal, P.]]
 [[Category: histidine containing protein]]
@@ Line 20: / Line 20: @@
 [[Category: pts]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:10:15 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:45 2008''