English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/87606
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:

Title

(1)H, (13)C and (15)N assignments of CdnL, an essential protein in Myxococcus xanthus

AuthorsMirassou, Yasmina ; Elías-Arnanz, Montserrat; Padmanabhan, Subramanian ; Jiménez, M. Angeles
KeywordsCdnL
CarD
PF02559
NMR
Myxococcus xanthus
Issue Date2013
PublisherSpringer
CitationBiomolecular NMR Assignments 7 (1): 51-55(2013)
AbstractCdnL, an essential protein in Myxococcus xanthus and several other bacteria, is a member of the large CarD_TRCF family of bacterial proteins that interact with RNA polymerase. Structural analyses of the 164-residue M. xanthus CdnL by NMR is complicated because of broadening, and hence overlap, of the signals due to the self-association and the monomer–dimer equilibrium that occurs in solution. Here, we report 1H, 13C and 15N assignments for CdnL achieved by analyzing its NMR spectra on the basis of the complete assignment obtained in this study for the 68-residue N-terminal fragment of CdnL (CdnLNt) together with those we described previously for the stable, protease-resistant, 110-residue C-terminal domain (CdnLCt). This approach relied on our observation that many of the CdnLNt and CdnLCt chemical shifts matched closely with those of the equivalent residues in the full-length protein. Our assignments provide the crucial first step in the structural analysis of CdnL and this functionally important family of bacterial proteins.
URIhttp://hdl.handle.net/10261/87606
DOI10.1007/s12104-012-9375-0
Identifiersdoi: 10.1007/s12104-012-9375-0
issn: 1874-270X
Appears in Collections:(IQFR) Artículos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.