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1ko7

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==X-ray structure of the HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 A resolution==
==X-ray structure of the HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 A resolution==
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<StructureSection load='1ko7' size='340' side='right' caption='[[1ko7]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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<StructureSection load='1ko7' size='340' side='right'caption='[[1ko7]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1ko7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29971 Atcc 29971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KO7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KO7 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1ko7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_xylosus Staphylococcus xylosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KO7 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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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]] 1.95&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HPRK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1288 ATCC 29971])</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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ko7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ko7 OCA], [http://pdbe.org/1ko7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ko7 RCSB], [http://www.ebi.ac.uk/pdbsum/1ko7 PDBsum]</span></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=1ko7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ko7 OCA], [https://pdbe.org/1ko7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ko7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ko7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ko7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/HPRK_STAXY HPRK_STAXY]] Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of 'Ser-46' in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The two antagonistic activities of HprK/P are regulated by several intracellular metabolites, which change their concentration in response to the absence or presence of rapidly metabolisable carbon sources (glucose, fructose, etc.) in the growth medium. Therefore, by controlling the phosphorylation state of HPr, the HprK/P is a sensor enzyme that plays a major role in the regulation of carbon metabolism and sugar transport: it mediates carbon catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate uptake and inducer exclusion.
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[https://www.uniprot.org/uniprot/HPRK_STAXY HPRK_STAXY] Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of 'Ser-46' in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The two antagonistic activities of HprK/P are regulated by several intracellular metabolites, which change their concentration in response to the absence or presence of rapidly metabolisable carbon sources (glucose, fructose, etc.) in the growth medium. Therefore, by controlling the phosphorylation state of HPr, the HprK/P is a sensor enzyme that plays a major role in the regulation of carbon metabolism and sugar transport: it mediates carbon catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate uptake and inducer exclusion.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ko/1ko7_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ko/1ko7_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
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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=1ko7 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 29971]]
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[[Category: Large Structures]]
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[[Category: Fieulaine, S]]
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[[Category: Staphylococcus xylosus]]
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[[Category: Hasenbein, S]]
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[[Category: Fieulaine S]]
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[[Category: Hengstenberg, W]]
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[[Category: Hasenbein S]]
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[[Category: Koch, B]]
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[[Category: Hengstenberg W]]
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[[Category: Marquez, J A]]
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[[Category: Koch B]]
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[[Category: Nessler, S]]
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[[Category: Marquez JA]]
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[[Category: Scheffzek, K]]
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[[Category: Nessler S]]
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[[Category: Dual activity]]
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[[Category: Scheffzek K]]
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[[Category: Hydrolase]]
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[[Category: Phosphotransfer]]
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[[Category: Product]]
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[[Category: Protein kinase]]
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[[Category: Protein phosphatase]]
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[[Category: Substrate]]
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[[Category: Transferase]]
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Current revision

X-ray structure of the HPr kinase/phosphatase from Staphylococcus xylosus at 1.95 A resolution

PDB ID 1ko7

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