English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/114848
Compartir / Impacto:
Estadísticas
Add this article to your Mendeley library MendeleyBASE
Citado 6 veces en Web of Knowledge®  |  Pub MebCentral Ver citas en PubMed Central  |  Ver citas en Google académico
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar otros formatos: Exportar EndNote (RIS)Exportar EndNote (RIS)Exportar EndNote (RIS)
Título

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

Autor López-Estepa, Miguel ; Ardá, Ana ; Savko, Martin; Round, Adam; Shepard, William E.; Bruix, M. ; Coll, Miquel ; Fernández, Francisco J. ; Jiménez-Barbero, Jesús ; Vega, María Cristina
Fecha de publicación 21-abr-2015
EditorPublic Library of Science
Citación PLoS ONE 10(4): e0118606
ResumenCyclic 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.
Descripción 22 p.-10 fig.-1 tab.-5 fig. supl.-2 tab. supl._1 text. supl.
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
Versión del editorhttp://dx.doi.org/ 10.1371/journal.pone.0118606
http://dx.doi.org/10.1371/journal.pone.0134070
URI http://hdl.handle.net/10261/114848
DOI10.1371/journal.pone.0118606
10.1371/journal.pone.0134070
ISSN1932-6203
E-ISSN1932-6203
Aparece en las colecciones: (CIB) Artículos
(IBMB) Artículos
(IQFR) Artículos
Mostrar el registro completo
 



NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.