2hro

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(New page: 200px<br /><applet load="2hro" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hro, resolution 2.50&Aring;" /> '''Structure of the ful...)
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[[Image:2hro.gif|left|200px]]<br /><applet load="2hro" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2hro, resolution 2.50&Aring;" />
 
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'''Structure of the full-lenght Enzyme I of the PTS system from Staphylococcus carnosus'''<br />
 
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==Overview==
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==Structure of the full-lenght Enzyme I of the PTS system from Staphylococcus carnosus==
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Enzyme I (EI) is the phosphoenolpyruvate (PEP)-protein phosphotransferase, at the entry point of the PEP-dependent sugar phosphotransferase system, which catalyzes carbohydrate uptake into bacterial cells. In the first, step of this pathway EI phosphorylates the heat-stable phospho carrier, protein at His-15 using PEP as a phosphoryl donor in a reaction that, requires EI dimerization and autophosphorylation at His-190. The structure, of the full-length protein from Staphylococcus carnosus at 2.5A reveals an, extensive interaction surface between two molecules in adjacent asymmetric, units. Structural comparison with related domains indicates that this, surface represents the biochemically relevant contact area of dimeric EI., Each monomer has an extended configuration with the phosphohistidine and, heat-stable phospho carrier protein-binding domains clearly separated from, the C-terminal dimerization and PEP-binding region. The large distance of, more than 35A between the active site His-190 and the PEP binding site, suggests that large conformational changes must occur during the process, of autophosphorylation, as has been proposed for the structurally related, enzyme pyruvate phosphate dikinase. Our structure for the first time, offers a framework to analyze a large amount of research in the context of, the full-length model.
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<StructureSection load='2hro' size='340' side='right'caption='[[2hro]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2hro]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_carnosus Staphylococcus carnosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HRO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HRO FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hro OCA], [https://pdbe.org/2hro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hro RCSB], [https://www.ebi.ac.uk/pdbsum/2hro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hro ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PT1_STACT PT1_STACT] 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. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hr/2hro_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2hro ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2HRO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_carnosus Staphylococcus carnosus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phosphoenolpyruvate--protein_phosphotransferase Phosphoenolpyruvate--protein phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.9 2.7.3.9] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HRO OCA].
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*[[Phosphotransferase 3D structures|Phosphotransferase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure of the full-length enzyme I of the phosphoenolpyruvate-dependent sugar phosphotransferase system., Marquez J, Reinelt S, Koch B, Engelmann R, Hengstenberg W, Scheffzek K, J Biol Chem. 2006 Oct 27;281(43):32508-15. Epub 2006 Jul 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16867985 16867985]
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[[Category: Large Structures]]
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[[Category: Phosphoenolpyruvate--protein phosphotransferase]]
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[[Category: Single protein]]
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[[Category: Staphylococcus carnosus]]
[[Category: Staphylococcus carnosus]]
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[[Category: Engelman, R.]]
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[[Category: Engelman R]]
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[[Category: Hengstenberg, W.]]
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[[Category: Hengstenberg W]]
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[[Category: Koch, B.]]
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[[Category: Koch B]]
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[[Category: Marquez, J.A.]]
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[[Category: Marquez JA]]
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[[Category: Reinelt, S.]]
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[[Category: Reinelt S]]
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[[Category: Scheffzek, K.]]
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[[Category: Scheffzek K]]
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[[Category: SO4]]
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[[Category: histidine phosphorylation]]
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[[Category: protein phosphorylation]]
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[[Category: pts]]
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[[Category: sugar transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:55:59 2007''
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Current revision

Structure of the full-lenght Enzyme I of the PTS system from Staphylococcus carnosus

PDB ID 2hro

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