4KBJ

Structure of Mtb RNAP Beta subunit B1 and B2 domains

Summary for 4KBJ

• Entry DOI: 10.2210/pdb4kbj/pdb
• Descriptor: DNA-directed RNA polymerase subunit beta (2 entities in total)
• Functional Keywords: structural genomics, tb structural genomics consortium, tbsgc, dna dependent rna polymerase, card, trcf, sigma factors, dna, transferase
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 2
• Total formula weight: 92532.65

Authors

Gulten, G.,Sacchettini, J.C.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2013-04-23, release date: 2013-10-02, Last modification date: 2024-02-28)

Primary citation

Gulten, G.,Sacchettini, J.C.
Structure of the Mtb CarD/RNAP beta-Lobes Complex Reveals the Molecular Basis of Interaction and Presents a Distinct DNA-Binding Domain for Mtb CarD.
Structure, 21:1859-1869, 2013

PubMed 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.

PubMed: 24055315
DOI: 10.1016/j.str.2013.08.014

Experimental method

X-RAY DIFFRACTION (2.4532 Å)