Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2LT1

Solution NMR structure of the 72-residue N-terminal domain of Myxococcus xanthus CarD

Summary for 2LT1
Entry DOI10.2210/pdb2lt1/pdb
NMR InformationBMRB: 18194
DescriptorCarD protein (1 entity in total)
Functional Keywordscard, cdnl, trcf-rid, pf02559, transcription
Biological sourceMyxococcus xanthus
Total number of polymer chains1
Total formula weight7889.12
Authors
Jimenez, M.A.,Padmanabhan, S. (deposition date: 2012-05-10, release date: 2013-11-13, Last modification date: 2024-05-15)
Primary citationBernal-Bernal, D.,Gallego-Garcia, A.,Garcia-Martinez, G.,Garcia-Heras, F.,Jimenez, M.A.,Padmanabhan, S.,Elias-Arnanz, M.
Structure-Function Dissection of Myxococcus xanthus CarD N-Terminal Domain, a Defining Member of the CarD_CdnL_TRCF Family of RNA Polymerase Interacting Proteins.
Plos One, 10:e0121322-e0121322,
Cited by
PubMed Abstract: Two prototypes of the large CarD_CdnL_TRCF family of bacterial RNA polymerase (RNAP)-binding proteins, Myxococcus xanthus CarD and CdnL, have distinct functions whose molecular basis remain elusive. CarD, a global regulator linked to the action of several extracytoplasmic function (ECF) σ-factors, binds to the RNAP β subunit (RNAP-β) and to protein CarG via an N-terminal domain, CarDNt, and to DNA via an intrinsically unfolded C-terminal domain resembling eukaryotic high-mobility-group A (HMGA) proteins. CdnL, a CarDNt-like protein that is essential for cell viability, is implicated in σA-dependent rRNA promoter activation and interacts with RNAP-β but not with CarG. While the HMGA-like domain of CarD by itself is inactive, we find that CarDNt has low but observable ability to activate ECF σ-dependent promoters in vivo, indicating that the C-terminal DNA-binding domain is required to maximize activity. Our structure-function dissection of CarDNt reveals an N-terminal, five-stranded β -sheet Tudor-like domain, CarD1-72, whose structure and contacts with RNAP-β mimic those of CdnL. Intriguingly, and in marked contrast to CdnL, CarD mutations that disrupt its interaction with RNAP-β did not annul activity. Our data suggest that the CarDNt C-terminal segment, CarD61-179, may be structurally distinct from its CdnL counterpart, and that it houses at least two distinct and crucial function determinants: (a) CarG-binding, which is specific to CarD; and (b) a basic residue stretch, which is also conserved and functionally required in CdnL. This study highlights the evolution of shared and divergent interactions in similar protein modules that enable the distinct activities of two related members of a functionally important and widespread bacterial protein family.
PubMed: 25811865
DOI: 10.1371/journal.pone.0121322
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

227561

PDB entries from 2024-11-20

PDB statisticsPDBj update infoContact PDBjnumon