2mp0: Difference between revisions
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==Protein Phosphorylation upon a Fleeting Encounter== | ==Protein Phosphorylation upon a Fleeting Encounter== | ||
<StructureSection load='2mp0' size='340' side='right'caption='[[2mp0 | <StructureSection load='2mp0' size='340' side='right'caption='[[2mp0]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2mp0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2mp0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MP0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MP0 FirstGlance]. <br> | ||
</td></tr><tr id=' | </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=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO3:PHOSPHITE+ION'>PO3</scene></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=2mp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mp0 OCA], [https://pdbe.org/2mp0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mp0 RCSB], [https://www.ebi.ac.uk/pdbsum/2mp0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mp0 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=2mp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mp0 OCA], [https://pdbe.org/2mp0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mp0 RCSB], [https://www.ebi.ac.uk/pdbsum/2mp0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mp0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/PT1_ECOLI PT1_ECOLI] 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).<ref>PMID:7876255</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli K-12]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Huang P]] | |||
[[Category: Huang | [[Category: Tang C]] | ||
[[Category: Tang | [[Category: Xing Q]] | ||
[[Category: Xing | [[Category: Yang J]] | ||
[[Category: Yang | [[Category: Zhang W]] | ||
[[Category: Zhang | |||
Revision as of 16:09, 26 July 2023
Protein Phosphorylation upon a Fleeting EncounterProtein Phosphorylation upon a Fleeting Encounter
Structural highlights
FunctionPT1_ECOLI 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).[1] Publication Abstract from PubMedProteins interact with each other to fulfill their functions. The importance of weak protein-protein interactions has been increasingly recognized. However, owing to technical difficulties, ultra-weak interactions remain to be characterized. Phosphorylation can take place via a K(D) approximately 25 mM interaction between two bacterial enzymes. Using paramagnetic NMR spectroscopy and with the introduction of a novel Gd(III)-based probe, we determined the structure of the resulting complex to atomic resolution. The structure accounts for the mechanism of phosphoryl transfer between the two enzymes and demonstrates the physical basis for their ultra-weak interaction. Further, molecular dynamics (MD) simulations suggest that the complex has a lifetime in the micro- to millisecond regimen. Hence such interaction is termed a fleeting interaction. From mathematical modeling, we propose that an ultra-weak fleeting interaction enables rapid flux of phosphoryl signal, providing a high effective protein concentration. Visualizing an ultra-weak protein-protein interaction in phosphorylation signaling.,Xing Q, Huang P, Yang J, Sun JQ, Gong Z, Dong X, Guo DC, Chen SM, Yang YH, Wang Y, Yang MH, Yi M, Ding YM, Liu ML, Zhang WP, Tang C Angew Chem Int Ed Engl. 2014 Oct 20;53(43):11501-5. doi: 10.1002/anie.201405976. , Epub 2014 Aug 11. PMID:25131700[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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