2qmh: Difference between revisions

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<StructureSection load='2qmh' size='340' side='right'caption='[[2qmh]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='2qmh' size='340' side='right'caption='[[2qmh]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2qmh]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_a"_von_freudenreich_1890 "bacillus a" von freudenreich 1890]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QMH FirstGlance]. <br>
<table><tr><td colspan='2'>[[2qmh]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Lacticaseibacillus_casei Lacticaseibacillus casei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QMH FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jb1|1jb1]], [[1kkl|1kkl]], [[1kkm|1kkm]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hprK ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1582 "Bacillus a" von Freudenreich 1890])</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=2qmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qmh OCA], [https://pdbe.org/2qmh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qmh RCSB], [https://www.ebi.ac.uk/pdbsum/2qmh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qmh 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=2qmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qmh OCA], [https://pdbe.org/2qmh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qmh RCSB], [https://www.ebi.ac.uk/pdbsum/2qmh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qmh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/HPRK_LACCA HPRK_LACCA]] 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, 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.[HAMAP-Rule:MF_01249]  
[https://www.uniprot.org/uniprot/HPRK_LACCA HPRK_LACCA] 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, 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.[HAMAP-Rule:MF_01249]
== 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: Bacillus a von freudenreich 1890]]
[[Category: Lacticaseibacillus casei]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chaptal, V]]
[[Category: Chaptal V]]
[[Category: Deutscher, J]]
[[Category: Deutscher J]]
[[Category: Gueguen-Chaignon, V]]
[[Category: Gueguen-Chaignon V]]
[[Category: Morera, S]]
[[Category: Morera S]]
[[Category: Nessler, S]]
[[Category: Nessler S]]
[[Category: Poncet, S]]
[[Category: Poncet S]]
[[Category: Vincent, F]]
[[Category: Vincent F]]
[[Category: Atp-binding]]
[[Category: Carbohydrate metabolism]]
[[Category: Kinase]]
[[Category: Magnesium]]
[[Category: Metal binding protein]]
[[Category: Metal-binding]]
[[Category: Multifunctional enzyme]]
[[Category: Nucleotide-binding]]
[[Category: Serine/threonine-protein kinase]]
[[Category: Transferase]]
[[Category: V267f mutation]]
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