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dc.contributor.authorTremino-Agulló, Lorenaes_ES
dc.contributor.authorForcada-Nadal, Aliciaes_ES
dc.contributor.authorContreras, Asunciónes_ES
dc.contributor.authorRubio, Vicentees_ES
dc.date.accessioned2017-10-31T07:48:35Z-
dc.date.available2017-10-31T07:48:35Z-
dc.date.issued2017-10-01-
dc.identifier.citationFEBS Letters 591(20):3431-3442 (2017)es_ES
dc.identifier.issn0014-5793-
dc.identifier.urihttp://hdl.handle.net/10261/156906-
dc.description12 páginas, 3 figurases_ES
dc.description.abstractThe Synechococcus elongatus COG0325 gene pipY functionally interacts with the nitrogen regulatory gene pipX. As a first step toward a molecular understanding of such interactions, we characterized PipY. This 221-residue protein is monomeric and hosts pyridoxal phosphate (PLP), binding it with limited affinity and losing it upon incubation with D-cycloserine. PipY crystal structures with and without PLP reveal a single-domain monomer folded as the TIM barrel of type-III fold PLP enzymes, with PLP highly exposed, fitting a role for PipY in PLP homeostasis. The mobile PLP phosphate-anchoring C-terminal helix might act as a trigger for PLP exchange. Exploiting the universality of COG0325 functions, we used PipY in site-directed mutagenesis studies to shed light on disease causation by epilepsy-associated mutations in the human COG0325 gene PROSC.es_ES
dc.description.sponsorshipSupported by grants from the Valencian Government (PrometeoII/2014/029) and Spanish Governments (BFU2014-58229-P to V.R.; BFU2012-33364 and BFU2015-66360-P to A.C.; FPI contract to LT) and to EC FP7/2007-2013 BioStruct-X (grant agreement N°283570, proposal 7687) for synchrotron access.es_ES
dc.language.isoenges_ES
dc.publisherWiley-Blackwelles_ES
dc.relationMINECO/BFU2014/58229-Pes_ES
dc.relationMINECO/BFU2012/33364es_ES
dc.relationMINECO/BFU2015/66360-Pes_ES
dc.relation.isversionofPostprintes_ES
dc.rightsopenAccessen_EN
dc.subjectSynechococcus elongatus PCC7942es_ES
dc.subjectCOG0325es_ES
dc.subjectPyridoxal phosphate proteinses_ES
dc.titleStudies on cyanobacterial protein PipY shed light on structure, potential functions, and vitamin B6 -dependent epilepsy.es_ES
dc.typeartículoes_ES
dc.identifier.doi10.1002/1873-3468.12841-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1002/1873-3468.12841es_ES
dc.identifier.e-issn1873-3468-
dc.embargo.terms2018-01-10es_ES
dc.contributor.funderGeneralitat Valencianaes_ES
dc.contributor.funderMinisterio de Economía y Competitividad (España)es_ES
dc.relation.csices_ES
oprm.item.hasRevisionno ko 0 false*
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003359es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
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