<p>(<b>A</b>) Sequence alignment of <i>M</i>. <i>xanthus</i> CarD and CdnL (NCBI accession codes CAA91224 and YP_630846, respectively). CarDNt corresponds to the 179-residue N-terminal CarD segment enclosed by the dashed line, and the remaining C-terminal segment to the HMGA-like region (with the four RGRP AT-hooks boxed). Arrowheads point to CarDNt residues analyzed by site-directed mutagenesis in this study. Below the sequence, arrows correspond to β-strands, the short black rod to a 3<sub>10</sub> helix and the grey rods to α-helices in the NMR solution structure determined for CdnL [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0121322#pone.0121322.ref010" target="_blank">10</a>]. (<b>B</b>) Schematic showing Car...
<p>Sequence alignment of (A) NOD1 and (B) RIP2 CARDs highlights the key residues that drive CARD-CAR...
<p>(<b>A</b>) Scheme of the strategy employed to check for <i>cdnL</i> complementation in <i>M. xant...
6 pages, 5 figures.-- PMID: 19666574 [PubMed].-- PMCID: PMC2726384.-- Supporting information (SI Mat...
<p>(<b>A</b>) Far UV-CD spectra of CarDNt (red) and CdnL (black). (<b>B</b>) 2D [<sup>1</sup>H,<sup>...
<p>(<b>A</b>) Ribbon representation of the average CarD<sub>1–72</sub> NMR solution structure showin...
<div><p>Two prototypes of the large CarD_CdnL_TRCF family of bacterial RNA polymerase (RNAP)-binding...
Two prototypes of the large CarD_CdnL_TRCF family of bacterial RNA polymerase (RNAP)-binding protein...
The CarD-CarG complex controls various cellular processes in the bacteriumMyxococcus xanthus includi...
CdnL and CarD are two functionally distinct members of the CarD_CdnL_TRCF family of bacterial RNA po...
© 2014 Gallego-García et al. CdnL and CarD are two functionally distinct members of the CarD-CdnL-TR...
CdnL, an essential protein in Myxococcus xanthus and several other bacteria, is a member of the larg...
<p>(A) Alignment of <i>Pseudomonas</i> MvaT with members of the H-NS family reveals regions of simil...
<p>(<b>A</b>) Native CdnLNt structure showing residue side chains that may contact RNAP-β, with the ...
<p>A Multiple sequence alignment of NLR and Apaf-1 CARD domains. Acidic key residues participating i...
Suppressor strains were sequenced with the Illumina MiSeq platform and compared to the annotated M. ...
<p>Sequence alignment of (A) NOD1 and (B) RIP2 CARDs highlights the key residues that drive CARD-CAR...
<p>(<b>A</b>) Scheme of the strategy employed to check for <i>cdnL</i> complementation in <i>M. xant...
6 pages, 5 figures.-- PMID: 19666574 [PubMed].-- PMCID: PMC2726384.-- Supporting information (SI Mat...
<p>(<b>A</b>) Far UV-CD spectra of CarDNt (red) and CdnL (black). (<b>B</b>) 2D [<sup>1</sup>H,<sup>...
<p>(<b>A</b>) Ribbon representation of the average CarD<sub>1–72</sub> NMR solution structure showin...
<div><p>Two prototypes of the large CarD_CdnL_TRCF family of bacterial RNA polymerase (RNAP)-binding...
Two prototypes of the large CarD_CdnL_TRCF family of bacterial RNA polymerase (RNAP)-binding protein...
The CarD-CarG complex controls various cellular processes in the bacteriumMyxococcus xanthus includi...
CdnL and CarD are two functionally distinct members of the CarD_CdnL_TRCF family of bacterial RNA po...
© 2014 Gallego-García et al. CdnL and CarD are two functionally distinct members of the CarD-CdnL-TR...
CdnL, an essential protein in Myxococcus xanthus and several other bacteria, is a member of the larg...
<p>(A) Alignment of <i>Pseudomonas</i> MvaT with members of the H-NS family reveals regions of simil...
<p>(<b>A</b>) Native CdnLNt structure showing residue side chains that may contact RNAP-β, with the ...
<p>A Multiple sequence alignment of NLR and Apaf-1 CARD domains. Acidic key residues participating i...
Suppressor strains were sequenced with the Illumina MiSeq platform and compared to the annotated M. ...
<p>Sequence alignment of (A) NOD1 and (B) RIP2 CARDs highlights the key residues that drive CARD-CAR...
<p>(<b>A</b>) Scheme of the strategy employed to check for <i>cdnL</i> complementation in <i>M. xant...
6 pages, 5 figures.-- PMID: 19666574 [PubMed].-- PMCID: PMC2726384.-- Supporting information (SI Mat...