1ka5: Difference between revisions

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 ==Refined Solution Structure of Histidine Containing Phosphocarrier Protein from Staphyloccocus aureus==
-<StructureSection load='1ka5' size='340' side='right' caption='[[1ka5]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''>
+<StructureSection load='1ka5' size='340' side='right'caption='[[1ka5]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ka5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1zer 1zer]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KA5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KA5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ka5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1zer 1zer]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KA5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KA5 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zer|1zer]]</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=1ka5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ka5 OCA], [http://pdbe.org/1ka5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ka5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ka5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ka5 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=1ka5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ka5 OCA], [https://pdbe.org/1ka5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ka5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ka5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ka5 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PTHP_STAAU PTHP_STAAU]] 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_STAAU PTHP_STAAU] 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </div>
 <div class="pdbe-citations 1ka5" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Phosphocarrier protein HPr 3D structures|Phosphocarrier protein HPr 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Staphylococcus aureus]]
-[[Category: Hengstenberg, W]]
+[[Category: Hengstenberg W]]
-[[Category: Kalbitzer, H R]]
+[[Category: Kalbitzer HR]]
-[[Category: Maurer, T]]
+[[Category: Maurer T]]
-[[Category: Meier, S]]
+[[Category: Meier S]]
-[[Category: SPINE, Structural Proteomics in Europe]]
-[[Category: Ligand transport]]
-[[Category: Open faced beta-sandwich]]
-[[Category: Spine]]
-[[Category: Structural genomic]]
-[[Category: Structural proteomics in europe]]