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[[Image:1opd.gif|left|200px]]<br />
<applet load="1opd" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1opd, resolution 1.5&Aring;" />
'''HISTIDINE-CONTAINING PROTEIN (HPR), MUTANT WITH SER 46 REPLACED BY ASP (S46D)'''<br />


==Overview==
==HISTIDINE-CONTAINING PROTEIN (HPR), MUTANT WITH SER 46 REPLACED BY ASP (S46D)==
Histidine-containing protein (HPr) is a phosphocarrier protein of the, bacterial phosphoenolpyruvate:sugar phosphotransferase system. HPr is, phosphorylated at the active site residue, His15, by, phosphoenolpyruvate-dependent enzyme I in the first enzyme reaction in the, process of phosphoryl transfer to sugar. In many Gram-positive bacterial, species HPr may also be phosphorylated at Ser46 by an ATP-dependent, protein kinase but not in the Gram-negative Escherichia coli and, Salmonella typhimurium. One effect of the phosphorylation at Ser46 is to, make HPr a poor acceptor for phosphorylation at His15. In Bacillus, subtilis HPr, the mutation Ser46Asp mimics the effects of phosphorylation., A series of mutations were made at Ser46 in E. coli HPr: Ala, Arg, Asn, Asp, Glu, and Gly. The two ... [[http://ispc.weizmann.ac.il/pmbin/getpm?8784179 (full description)]]
<StructureSection load='1opd' size='340' side='right'caption='[[1opd]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1opd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OPD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1opd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1opd OCA], [https://pdbe.org/1opd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1opd RCSB], [https://www.ebi.ac.uk/pdbsum/1opd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1opd 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/op/1opd_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=1opd ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1OPD 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 SO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Sites: ACT and AS6. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OPD OCA]].
*[[Phosphocarrier protein HPr 3D structures|Phosphocarrier protein HPr 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Mutation of serine-46 to aspartate in the histidine-containing protein of Escherichia coli mimics the inactivation by phosphorylation of serine-46 in HPrs from gram-positive bacteria., Napper S, Anderson JW, Georges F, Quail JW, Delbaere LT, Waygood EB, Biochemistry. 1996 Sep 3;35(35):11260-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8784179 8784179]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Delbaere, L.]]
[[Category: Delbaere L]]
[[Category: Napper, S.]]
[[Category: Napper S]]
[[Category: Waygood, B.]]
[[Category: Waygood B]]
[[Category: SO4]]
[[Category: histidine]]
[[Category: phosphotransferase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:58:17 2007''

Latest revision as of 11:02, 14 February 2024

HISTIDINE-CONTAINING PROTEIN (HPR), MUTANT WITH SER 46 REPLACED BY ASP (S46D)HISTIDINE-CONTAINING PROTEIN (HPR), MUTANT WITH SER 46 REPLACED BY ASP (S46D)

Structural highlights

1opd is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
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

1opd, resolution 1.50Å

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