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==Solution structure of the active-centre mutant Ile14Ala of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus carnosus==
==Solution structure of the active-centre mutant Ile14Ala of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus carnosus==
<StructureSection load='1txe' size='340' side='right'caption='[[1txe]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
<StructureSection load='1txe' size='340' side='right'caption='[[1txe]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1txe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51365 Atcc 51365]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TXE FirstGlance]. <br>
<table><tr><td colspan='2'>[[1txe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_carnosus Staphylococcus carnosus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TXE FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qr5|1qr5]]</td></tr>
</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='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=1txe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1txe OCA], [http://pdbe.org/1txe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1txe RCSB], [http://www.ebi.ac.uk/pdbsum/1txe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1txe ProSAT]</span></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=1txe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1txe OCA], [https://pdbe.org/1txe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1txe RCSB], [https://www.ebi.ac.uk/pdbsum/1txe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1txe ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PTHP_STACA PTHP_STACA]] 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).  P-Ser-HPr interacts with the catabolite control protein A (CcpA), forming a complex that binds to DNA at the catabolite response elements cre, operator sites preceding a large number of catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite repression (CCR), a mechanism that allows bacteria to coordinate and optimize the utilization of available carbon sources. P-Ser-HPr also plays a role in inducer exclusion, in which it probably interacts with several non-PTS permeases and inhibits their transport activity (By similarity).  
[https://www.uniprot.org/uniprot/PTHP_STACA PTHP_STACA] 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).  P-Ser-HPr interacts with the catabolite control protein A (CcpA), forming a complex that binds to DNA at the catabolite response elements cre, operator sites preceding a large number of catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite repression (CCR), a mechanism that allows bacteria to coordinate and optimize the utilization of available carbon sources. P-Ser-HPr also plays a role in inducer exclusion, in which it probably interacts with several non-PTS permeases and inhibits their transport activity (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 51365]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Brunner, E]]
[[Category: Staphylococcus carnosus]]
[[Category: Hengstenberg, W]]
[[Category: Brunner E]]
[[Category: Kalbitzer, H R]]
[[Category: Hengstenberg W]]
[[Category: Koch, B]]
[[Category: Kalbitzer HR]]
[[Category: Moeglich, A]]
[[Category: Koch B]]
[[Category: SPINE, Structural Proteomics in Europe]]
[[Category: Moeglich A]]
[[Category: Open-faced beta-sandwich]]
[[Category: Spine]]
[[Category: Structural genomic]]
[[Category: Structural proteomics in europe]]
[[Category: Transport protein]]

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