1pfh: Difference between revisions

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New page: left|200px<br /><applet load="1pfh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pfh" /> '''THE PHOSPHORYLATED FORM OF THE HISTIDINE-CON...
 
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[[Image:1pfh.jpg|left|200px]]<br /><applet load="1pfh" size="450" color="white" frame="true" align="right" spinBox="true"
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'''THE PHOSPHORYLATED FORM OF THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR'''<br />


==Overview==
==THE PHOSPHORYLATED FORM OF THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR==
The solution structure of the phosphorylated form of the, histidine-containing phosphocarrier protein, HPr, from Escherichia coli, has been determined by NMR in combination with restrained molecular, dynamics simulations. The structure of phospho-HPr (P-HPr) results from a, molecular dynamics simulation in water, using time-dependent distance, restraints to attain agreement with the measured NOEs. Experimental, restraints were identified from both three-dimensional 1H-1H-15N, HSQC-NOESY and two-dimensional 1H-1HNOESY spectra, and compared with those, of the unphosphorylated form. Structural changes upon phosphorylation of, HPr are limited to the active site, as evidenced by changes in chemical, shifts, in 3JNHH alpha-coupling constants and NOE patterns. Chemical shift, changes were obtained mainly for protons that were positioned close to the, phosphoryl group attached to the His15 imidazole ring. Differences could, be detected in the intensity of the NOEs involving the side-chain protons, of His15 and Pro18, resulting from a change in the relative position of, the two rings. In addition, a small change could be detected in the, three-bond J-coupling between the amide proton and the H alpha proton of, Thr16 and Arg17 upon phosphorylation, in agreement with the changes of the, phi torsion angle of these two residues obtained from time-averaged, restrained molecular dynamics simulations in water. The proposed role of, the torsion-angle strain at residue 16 in the mechanism of Streptococcus, faecalis HPr is not supported by these results. In contrast, phosphorylation seems to introduce torsion angle strain at residue His15., This strain could facilitate the transfer of the phosphoryl group to the, A-domain at enzyme II. The phospho-histidine is not stabilised by hydrogen, bonds to the side-chain group of Arg17; instead stable hydrogen bonds are, formed between the phosphate group and the backbone amide protons of Thr16, and Arg17, which show the largest changes in chemical shift upon, phosphorylation, and a hydrogen bond involving the side-chain O gamma, proton of Thr16. HPr accepts the phosphoryl group from enzyme I and, donates it subsequently to the A domain of various enzyme II species. The, binding site for EI on HPr resembles that of the A domain of the, mannitol-specific enzyme II, as can be concluded from the changes on the, amide proton and nitrogen chemical shifts observed via heteromolecular, single-quantum coherence spectroscopy.
<StructureSection load='1pfh' size='340' side='right'caption='[[1pfh]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1pfh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PFH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HIP:ND1-PHOSPHONOHISTIDINE'>HIP</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pfh OCA], [https://pdbe.org/1pfh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pfh RCSB], [https://www.ebi.ac.uk/pdbsum/1pfh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pfh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PTHP_ECOLI PTHP_ECOLI] General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the permease (enzymes II/III).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pf/1pfh_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1pfh ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1PFH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PHS as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PFH OCA].
*[[Phosphocarrier protein HPr 3D structures|Phosphocarrier protein HPr 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
High-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from NMR-NOE data., van Nuland NA, Boelens R, Scheek RM, Robillard GT, J Mol Biol. 1995 Feb 10;246(1):180-93. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7853396 7853396]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Nuland, N.A.J.Van.]]
[[Category: Robillard GT]]
[[Category: Robillard, G.T.]]
[[Category: Scheek RM]]
[[Category: Scheek, R.M.]]
[[Category: Van Nuland NAJ]]
[[Category: PHS]]
[[Category: phosphocarrier protein]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:45:37 2007''

Latest revision as of 08:55, 17 April 2024

THE PHOSPHORYLATED FORM OF THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPRTHE PHOSPHORYLATED FORM OF THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR

Structural highlights

1pfh is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PTHP_ECOLI General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the permease (enzymes II/III).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

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