Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/155078
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Campo DC | Valor | Lengua/Idioma |
---|---|---|
dc.contributor.author | Palanca, Carles | es_ES |
dc.contributor.author | Rubio, Vicente | es_ES |
dc.date.accessioned | 2017-09-13T10:57:58Z | - |
dc.date.available | 2017-09-13T10:57:58Z | - |
dc.date.issued | 2017-04-12 | - |
dc.identifier.citation | Environmental Microbiology Reports 9(3):290-299 (2017) | es_ES |
dc.identifier.uri | http://hdl.handle.net/10261/155078 | - |
dc.description | 10 páginas, 3 figuras, 1 tabla | es_ES |
dc.description.abstract | To adapt to environments with variable nitrogen sources and richness, the widely distributed homotrimeric PII signalling proteins bind their allosteric effectors ADP/ATP/2-oxoglutarate, and experience nitrogen-sensitive uridylylation of their flexible T-loops at Tyr51, regulating their interactions with effector proteins. To clarify whether uridylylation triggers a given T-loop conformation, we determined the crystal structure of the classical paradigm of PII protein, Escherichia coli GlnB (EcGlnB), in fully uridylylated form (EcGlnB-UMP3 ). This is the first structure of a postranslationally modified PII protein. This required recombinant production and purification of the uridylylating enzyme GlnD and its use for full uridylylation of large amounts of recombinantly produced pure EcGlnB. Unlike crystalline non-uridylylated EcGlnB, in which T-loops are fixed, uridylylation rendered the T-loop highly mobile because of loss of contacts mediated by Tyr51, with concomitant abolition of T-loop anchoring via Arg38 on the ATP site. This site was occupied by ATP, providing the first, long-sought snapshot of the EcGlnB-ATP complex, connecting ATP binding with T-loop changes. Inferences are made on the mechanisms of PII selectivity for ATP and of PII-UMP3 signalling, proposing a model for the architecture of the complex of EcGlnB-UMP3 with the uridylylation-sensitive PII target ATase (which adenylylates/deadenylylates glutamine synthetase [GS]) and with GS. | es_ES |
dc.description.sponsorship | Supported by grants from the Valencian (PrometeoII/2014/029) and Spanish Governments (BFU2014-58229-P). CP was a JAE-Predoc fellow of the CSIC. The research leading to these results has received funding from the European Community’s Seventh Framework Programme (FP7/2007-2esrf13) under BioStruct-X (grant agreement N8283570), within proposal 7687 | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | Wiley-Blackwell | es_ES |
dc.relation | MINECO/BFU2014/58229-P) | es_ES |
dc.relation | info:eu-repo/grantAgreement/EC/FP7/2007-2esrf13/8283570 | es_ES |
dc.relation.isversionof | Postprint | es_ES |
dc.rights | openAccess | en_EN |
dc.subject | PII protein | es_ES |
dc.subject | X-ray crystallography | es_ES |
dc.subject | Signaling | es_ES |
dc.subject | ATase | es_ES |
dc.subject | Glutamine synthetase | es_ES |
dc.subject | Postranslational modification | es_ES |
dc.title | Effects of T-loop modification on the PII-signaling protein: Structure of uridylylated Escherichia coli GlnB bound to ATP | es_ES |
dc.type | artículo | es_ES |
dc.identifier.doi | 10.1111/1758-2229.12533 | - |
dc.description.peerreviewed | Peer reviewed | es_ES |
dc.relation.publisherversion | http://dx.doi.org/10.1111/1758-2229.12533 | es_ES |
dc.identifier.e-issn | 1758-2229 | - |
dc.embargo.terms | 2018-06-01 | es_ES |
dc.contributor.funder | Generalitat Valenciana | es_ES |
dc.contributor.funder | Ministerio de Economía y Competitividad (España) | es_ES |
dc.contributor.funder | European Economic Community | es_ES |
dc.relation.csic | Sí | es_ES |
oprm.item.hasRevision | no ko 0 false | * |
dc.identifier.funder | http://dx.doi.org/10.13039/501100003329 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/501100003359 | es_ES |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.languageiso639-1 | en | - |
item.fulltext | With Fulltext | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.cerifentitytype | Publications | - |
item.grantfulltext | open | - |
item.openairetype | artículo | - |
Aparece en las colecciones: | (IBV) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
2017 Environ Microbiol Rep 9 Vers Autor.pdf | 1,87 MB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
6
checked on 24-abr-2024
WEB OF SCIENCETM
Citations
6
checked on 26-feb-2024
Page view(s)
285
checked on 24-abr-2024
Download(s)
190
checked on 24-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.