Structure of the Mtb CarD/RNAP β-Lobes Complex Reveals the Molecular Basis of Interaction and Presents a Distinct DNA-Binding Domain for Mtb CarD | Academic Article individual record
abstract

CarD from Mycobacterium tuberculosis (Mtb) is an essential protein shown to be involved in stringent response through downregulation of rRNA and ribosomal protein genes. CarD interacts with the β-subunit of RNAP and this interaction is vital for Mtb's survival during the persistent infection state. We have determined the crystal structure of CarD in complex with the RNAP β-subunit β1 and β2 domains at 2.1 Å resolution. The structure reveals the molecular basis of CarD/RNAP interaction, providing a basis to further our understanding of RNAP regulation by CarD. The structural fold of the CarD N-terminal domain is conserved in RNAP interacting proteins such as TRCF-RID and CdnL, and displays similar interactions to the predicted homology model based on the TRCF/RNAP β1 structure. Interestingly, the structure of the C-terminal domain, which is required for complete CarD function in vivo, represents a distinct DNA-binding fold.

author list (cited authors)
Gulten, G., & Sacchettini, J. C.
publication date
2013
publisher
Elsevier BV Publisher
published in
Structure Journal
keywords
  • Models, Molecular
  • DNA-Binding Proteins
  • Protein Binding
  • Mycobacterium Tuberculosis
  • Binding Sites
  • Crystallography, X-Ray
  • Protein Structure, Quaternary
  • Protein Structure, Secondary
  • Bacterial Proteins
  • Hydrophobic And Hydrophilic Interactions
  • DNA-Directed RNA Polymerases
  • Protein Interaction Domains And Motifs
  • Hydrogen Bonding
altmetric score

3.35

citation count

25