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Stability and binding of the phosphorylated species of the N-terminal domain of enzyme I and the histidine phosphocarrier protein from the Streptomyces coelicolor phosphoenolpyruvate:sugar phosphotransferase system
dc.contributor.author | Domenech, R | |
dc.contributor.author | Martínez Gómez, Ana Isabel | |
dc.contributor.author | Aguado Llera, D | |
dc.contributor.author | Martínez Rodríguez, Sergio | |
dc.contributor.author | Clemente Jiménez, Josefa María | |
dc.contributor.author | Velazquez Campoy, A. | |
dc.contributor.author | Neira Faleiro, José Luis | |
dc.date.accessioned | 2024-05-22T09:00:10Z | |
dc.date.available | 2024-05-22T09:00:10Z | |
dc.date.issued | 2012 | |
dc.identifier.issn | 003-9861 | |
dc.identifier.uri | http://hdl.handle.net/10835/16508 | |
dc.description.abstract | The phosphotransferase system (PTS) is involved in the use of carbon sources in bacteria. It is formed by two general proteins: enzyme I (EI) and the histidine phosphocarrier (HPr), and various sugar-specific permeases. EI is formed by two domains, with the N-terminal domain (EIN) being responsible for the binding to HPr. In low-G + C Gram-positive bacteria, HPr becomes phosphorylated not only by phosphoenolpyruvate (PEP) at the active-site histidine, but also by ATP at a serine. In this work, we have characterized: (i) the stability and binding affinities between the active-site-histidine phosphorylated species of HPr and the EIN from Streptomyces coelicolor; and (ii) the stability and binding affinities of the species involving the phosphorylation at the regulatory serine of HPrsc. Our results show that the phosphorylated active-site species of both proteins are less stable than the unphosphorylated counterparts. Conversely, the Hpr-S47D, which mimics phosphorylation at the regulatory serine, is more stable than wild-type HPrsc due to helical N-capping effects, as suggested by the modeled structure of the protein. Binding among the phosphorylated and unphosphorylated species is always entropically driven, but the affinity and the enthalpy vary widely. | es_ES |
dc.language.iso | en | es_ES |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Protein folding | es_ES |
dc.subject | Fluorescence | es_ES |
dc.subject | Protein stability | es_ES |
dc.subject | Isothermal titration calorimetry | es_ES |
dc.subject | Circular dichroism | es_ES |
dc.subject | NMR | es_ES |
dc.title | Stability and binding of the phosphorylated species of the N-terminal domain of enzyme I and the histidine phosphocarrier protein from the Streptomyces coelicolor phosphoenolpyruvate:sugar phosphotransferase system | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es_ES |