Literature DB >> 19636935

1H, 13C and 15N backbone and side chain resonance assignments of the C-terminal domain of CdnL from Myxococcus xanthus.

Yasmina Mirassou1, Diana García-Moreno, Clara M Santiveri, Jorge Santoro, Montserrat Elías-Arnanz, S Padmanabhan, M Angeles Jiménez.   

Abstract

CdnL, a 164-residue protein essential for Myxococcus xanthus viability, is a member of a large family of bacterial proteins of unknown structure and function. Here, we report the (1)H, (13)C and (15)N backbone and side chain assignments for the stable C-terminal domain of CdnL identified by limited proteolysis.

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Year:  2008        PMID: 19636935     DOI: 10.1007/s12104-008-9128-2

Source DB:  PubMed          Journal:  Biomol NMR Assign        ISSN: 1874-270X            Impact factor:   0.746


  2 in total

1.  Structural insights into RNA polymerase recognition and essential function of Myxococcus xanthus CdnL.

Authors:  Aránzazu Gallego-García; Yasmina Mirassou; Diana García-Moreno; Montserrat Elías-Arnanz; María Angeles Jiménez; S Padmanabhan
Journal:  PLoS One       Date:  2014-10-01       Impact factor: 3.240

2.  Structure-function dissection of Myxococcus xanthus CarD N-terminal domain, a defining member of the CarD_CdnL_TRCF family of RNA polymerase interacting proteins.

Authors:  Diego Bernal-Bernal; Aránzazu Gallego-García; Gema García-Martínez; Francisco García-Heras; María Angeles Jiménez; S Padmanabhan; Montserrat Elías-Arnanz
Journal:  PLoS One       Date:  2015-03-26       Impact factor: 3.240

  2 in total

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