Structure of the Mtb CarD/RNAP -lobes complex reveals the molecular basis of interaction and presents a distinct DNA-binding domain for Mtb CarD. Academic Article

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 -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 -subunit 1 and 2 domains at 2.1 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 1 structure. Interestingly, the structure of the C-terminal domain, which is required for complete CarD function in vivo, represents a distinct DNA-binding fold.

authors

• Sacchettini, James

published proceedings

• Structure

altmetric score

• 3.35

author list (cited authors)

• Gulten, G., & Sacchettini, J. C.

citation count

• 28

complete list of authors

• Gulten, Gulcin||Sacchettini, James C

publication date

• October 2013

publisher

• Elsevier  Publisher

published in

• Folding & design  Journal
• Structure  Journal

keywords

• Bacterial Proteins
• Binding Sites
• Crystallography, X-Ray
• DNA-Binding Proteins
• DNA-Directed RNA Polymerases
• Hydrogen Bonding
• Hydrophobic And Hydrophilic Interactions
• Models, Molecular
• Mycobacterium Tuberculosis
• Protein Binding
• Protein Interaction Domains And Motifs
• Protein Structure, Quaternary
• Protein Structure, Secondary

PubMed Central ID

• 24055315

Digital Object Identifier (DOI)

• 10.1016/j.str.2013.08.014

start page

• 1859

end page

• 1869

volume

• 21

issue

• 10