The crystal structure and small-angleX-ray analysis of CsdL/TcdA reveal a new tRNA binding motif in the MoeB/E1 superfamily

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dc.contributor.author	López-Estepa, Miguel	-
dc.contributor.author	Ardá, Ana	-
dc.contributor.author	Savko, Martin	-
dc.contributor.author	Round, Adam	-
dc.contributor.author	Shepard, William E.	-
dc.contributor.author	Bruix, M.	-
dc.contributor.author	Coll, Miquel	-
dc.contributor.author	Fernández, Francisco J.	-
dc.contributor.author	Jiménez-Barbero, Jesús	-
dc.contributor.author	Vega, María Cristina	-
dc.date.accessioned	2015-05-07T10:47:46Z	-
dc.date.available	2015-05-07T10:47:46Z	-
dc.date.issued	2015-04-21	-
dc.identifier.citation	PLoS ONE 10(4): e0118606	es_ES
dc.identifier.issn	1932-6203	-
dc.identifier.uri	http://hdl.handle.net/10261/114848	-
dc.description	22 p.-10 fig.-1 tab.-5 fig. supl.-2 tab. supl._1 text. supl.	es_ES
dc.description	View correction information of a table and other errors at López-Estepa M, Ardá A, Savko M, Round A, Shepard WE, et al. (2015) Correction: The Crystal Structure and Small-Angle X-Ray Analysis of CsdL/TcdA Reveal a New tRNA Binding Motif in the MoeB/E1 Superfamily. PLoS ONE 10(7): e0134070. doi: 10.1371/journal.pone.0134070	-
dc.description.abstract	Cyclic N6-threonylcarbamoyladenosine (‘cyclic t6A’, ct6 A) is a non-thiolated hypermodification found in transfer RNAs (tRNAs) in bacteria, protists, fungi and plants. In bacteria and yeast cells ct6 A has been shown to enhance translation fidelity and efficiency of ANN codons by improving the faithful discrimination of aminoacylated tRNAs by the ribosome. To further the understanding of ct6A biology we have determined the high-resolution crystal structures of CsdL/TcdA in complex with AMP and ATP, an E1-like activating enzyme from Escherichia coli, which catalyzes the ATP-dependent dehydration of t6A to form ct6 A. CsdL/TcdA is a dimer whose structural integrity and dimer interface depend critically on strongly bound K+ and Na+ cations. By using biochemical assays and small-angle X-ray scattering we show that CsdL/TcdA can associate with tRNA with a 1:1 stoichiometry and with the proper position and orientation for the cyclization of t6A. Furthermore, we show by nuclear magnetic resonance that CsdL/TcdA engages in transient interactions with CsdA and CsdE, which, in the latter case, involve catalytically important residues. These short-lived interactions may underpin the precise channeling of sulfur atoms from cysteine to CsdL/TcdA as previously characterized. In summary, the combination of structural, biophysical and biochemical methods applied to CsdL/TcdA has afforded a more thorough understanding of how the structure of this E1-like enzyme has been fine tuned to accomplish ct6A synthesis on tRNAs while providing support for the notion that CsdA and CsdE are able to functionally interact with CsdL/TcdA.	es_ES
dc.description.sponsorship	Ministerio de Economía y Competitividad (ES) (grants PET2008_0101, BIO2009-11184 and BFU2010-22260-C02-02 to MCV, BFU2008-02372/BMC, CONSOLIDER CSD 2006-23 and BFU2011-22588 to MC, CTQ2012-32035 to JJB), Generalitat de Catalunya (ES) (grant SGR2009-1309 to MC), the European Commission (Framework Programme 7 (FP7) projects ComplexINC No. 279039 to MCV and SILVER-GA No. 260644 to MC).	es_ES
dc.language.iso	eng	es_ES
dc.publisher	Public Library of Science	es_ES
dc.relation	info:eu-repo/grantAgreement/EC/FP7/283570	-
dc.relation.isversionof	Publisher's version	es_ES
dc.rights	openAccess	es_ES
dc.title	The crystal structure and small-angleX-ray analysis of CsdL/TcdA reveal a new tRNA binding motif in the MoeB/E1 superfamily	es_ES
dc.type	artículo	es_ES
dc.identifier.doi	10.1371/journal.pone.0118606	-
dc.identifier.doi	10.1371/journal.pone.0134070	-
dc.description.peerreviewed	Peer reviewed	es_ES
dc.relation.publisherversion	http://dx.doi.org/ 10.1371/journal.pone.0118606	es_ES
dc.relation.publisherversion	http://dx.doi.org/10.1371/journal.pone.0134070	-
dc.identifier.e-issn	1932-6203	-
dc.rights.license	http://creativecommons.org/licenses/by/4.0/	es_ES
dc.contributor.funder	Ministerio de Economía y Competitividad (España)	-
dc.contributor.funder	European Commission	-
dc.contributor.funder	Generalitat de Catalunya	-
dc.relation.csic	Sí	es_ES
dc.identifier.funder	http://dx.doi.org/10.13039/501100003329	es_ES
dc.identifier.funder	http://dx.doi.org/10.13039/501100000780	es_ES
dc.identifier.funder	http://dx.doi.org/10.13039/501100002809	es_ES
dc.identifier.pmid	25897750	-
dc.type.coar	http://purl.org/coar/resource_type/c_6501	es_ES
item.openairecristype	http://purl.org/coar/resource_type/c_18cf	-
item.fulltext	With Fulltext	-
item.cerifentitytype	Publications	-
item.openairetype	artículo	-
item.languageiso639-1	en	-
item.grantfulltext	open	-
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