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2n5t

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==Ensemble Solution structure of the phosphoenolpyruvate-Enzyme I complex from the bacterial hosphotransferase system==
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<StructureSection load='2n5t' size='340' side='right' caption='[[2n5t]], [[NMR_Ensembles_of_Models | 11 NMR models]]' scene=''>
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==Ensemble solution structure of the phosphoenolpyruvate-Enzyme I complex from the bacterial phosphotransferase system==
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<StructureSection load='2n5t' size='340' side='right'caption='[[2n5t]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2n5t]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N5T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N5T FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2n5t]] 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=2N5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N5T FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate--protein_phosphotransferase Phosphoenolpyruvate--protein phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.9 2.7.3.9] </span></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">Hybrid , Solution NMR , X-ray solution scattering</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=2n5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n5t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2n5t RCSB], [http://www.ebi.ac.uk/pdbsum/2n5t 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=2n5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n5t OCA], [https://pdbe.org/2n5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n5t RCSB], [https://www.ebi.ac.uk/pdbsum/2n5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n5t ProSAT]</span></td></tr>
</table>
</table>
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{{Large structure}}
 
== Function ==
== Function ==
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[[http://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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Enzyme I (EI) is the first component in the bacterial phosphotransferase system, a signal transduction pathway in which phosphoryl transfer through a series of bimolecular protein-protein interactions is coupled to sugar transport across the membrane. EI is a multidomain, 128-kDa homodimer that has been shown to exist in two conformational states related to one another by two large (50-90 degrees ) rigid body domain reorientations. The open conformation of apo EI allows phosphoryl transfer from His189 located in the N-terminal domain alpha/beta (EINalpha/beta) subdomain to the downstream protein partner bound to the EINalpha subdomain. The closed conformation, observed in a trapped phosphoryl transfer intermediate, brings the EINalpha/beta subdomain into close proximity to the C-terminal dimerization domain (EIC), thereby permitting in-line phosphoryl transfer from phosphoenolpyruvate (PEP) bound to EIC to His189. Here, we investigate the solution conformation of a complex of an active site mutant of EI (H189A) with PEP. Simulated annealing refinement driven simultaneously by solution small angle X-ray scattering and NMR residual dipolar coupling data demonstrates unambiguously that the EI(H189A)-PEP complex exists in a dynamic equilibrium between two approximately equally populated conformational states, one corresponding to the closed structure and the other to a partially closed species. The latter likely represents an intermediate in the open-to-closed transition.
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Dynamic equilibrium between closed and partially closed states of the bacterial Enzyme I unveiled by solution NMR and X-ray scattering.,Venditti V, Schwieters CD, Grishaev A, Clore GM Proc Natl Acad Sci U S A. 2015 Aug 24. pii: 201515366. PMID:26305976<ref>PMID:26305976</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Phosphoenolpyruvate--protein phosphotransferase]]
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[[Category: Escherichia coli K-12]]
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[[Category: Clore, G]]
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[[Category: Large Structures]]
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[[Category: Grishaev, A]]
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[[Category: Clore G]]
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[[Category: Schwieters, C D]]
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[[Category: Grishaev A]]
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[[Category: Venditti, V]]
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[[Category: Schwieters CD]]
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[[Category: Transferase]]
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[[Category: Venditti V]]

Current revision

Ensemble solution structure of the phosphoenolpyruvate-Enzyme I complex from the bacterial phosphotransferase system

PDB ID 2n5t

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