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dc.contributor.authorForcada-Nadal, Aliciaes_ES
dc.contributor.authorPalomino-Schätzlein, Martinaes_ES
dc.contributor.authorNeira, José L.es_ES
dc.contributor.authorPineda-Lucena, Antonioes_ES
dc.contributor.authorRubio, Vicentees_ES
dc.date.accessioned2017-10-16T10:48:41Z-
dc.date.available2017-10-16T10:48:41Z-
dc.date.issued2017-06-14-
dc.identifier.citationBiochemistry 56(25):3211-3224 (2017)es_ES
dc.identifier.issn0006-2960-
dc.identifier.urihttp://hdl.handle.net/10261/156304-
dc.description14 páginas, 8 figuras, 1 tablaes_ES
dc.description.abstractPipX, an 89-residue protein, acts as a co-activator of the global nitrogen regulator NtcA in cyanobacteria. NtcA-PipX interactions are regulated by 2-oxoglutarate (2-OG), an inverse indicator of the ammonia abundance, and by PII, a protein that binds to PipX at low 2-OG concentrations. The structure of PipX, when bound to NtcA or PII, consists of an N-terminal, five-stranded -sheet (conforming a Tudor-like domain), and two long -helices. These helices adopt either a flexed conformation, where they are in close contact and in an antiparallel mutual orientation, also packing against the -sheet; or an open conformation (observed only in the PII-PipX complex) where the last -helix moves apart from the rest of the protein. The aim of this work was to study the structure and dynamics of isolated PipX in solution by NMR. The backbone chemical shifts, the hydrogen-exchange and the NOE patterns indicated that the isolated, monomeric PipX structure was formed by an N-terminal five-stranded -sheet and two C-terminal -helices. Furthermore, the observed NOEs between the two helices, and of -helix2 with -strand2 suggested that PipX adopted a flexed conformation. The -strands 1 and 5 were highly flexible, as shown by the lack of inter-strand backbone-backbone NOEs; in addition, the 15N-dynamics indicated that the C terminus of -strand4 and the following -turn (Phe42-Thr47), and the C-cap of -helix1 (Arg70-Asn71) were particularly mobile. These two regions could act as hinges, allowing PipX to interact with its partners, including PlmA in the newly recognized PII-PipX-PlmA ternary complex.es_ES
dc.description.sponsorshipThis work was supported by the Spanish Ministerio de Economía y Competitividad (CTQ2013-4493-R to JLN; BFU2014-58229-P to VR) and by the Generalitat Valenciana (PrometeoII/2014/029 to VR).es_ES
dc.language.isoenges_ES
dc.publisherAmerican Chemical Societyes_ES
dc.relationMINECO/CTQ2013/4493-Res_ES
dc.relationMINECO/BFU2014/58229-Pes_ES
dc.relation.isversionofPostprintes_ES
dc.rightsopenAccessen_EN
dc.subjectDynamicses_ES
dc.subjectMobilityes_ES
dc.subjectNMRes_ES
dc.subjectPipXes_ES
dc.subjectRelaxationes_ES
dc.subjectStructurees_ES
dc.titleThe PipX protein, when not bound to its targets, has its signalling C-terminal helix in a flexed conformationes_ES
dc.typeartículoes_ES
dc.identifier.doi10.1021/acs.biochem.7b00230-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1021/acs.biochem.7b00230es_ES
dc.identifier.e-issn1520-4995-
dc.contributor.funderMinisterio de Economía, Industria y Competitividad (España)es_ES
dc.contributor.funderGeneralitat Valencianaes_ES
dc.relation.csices_ES
oprm.item.hasRevisionno ko 0 false*
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003359es_ES
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