4KBM
Structure of the Mtb CarD/RNAP Beta subunit B1-B2 domains complex
Summary for 4KBM
| Entry DOI | 10.2210/pdb4kbm/pdb |
| Related | 4KBJ |
| Descriptor | DNA-directed RNA polymerase subunit beta, RNA polymerase-binding transcription factor CarD (3 entities in total) |
| Functional Keywords | structural genomics, tb structural genomics consortium, tbsgc, tudor, dna-dependent rna polymerase, transcription regulator, protein-protein complex, card, dna, sigma factor, transferase-transcription complex, transferase/transcription |
| Biological source | Mycobacterium tuberculosis More |
| Total number of polymer chains | 2 |
| Total formula weight | 64199.68 |
| Authors | Gulten, G.,Sacchettini, J.C.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2013-04-23, release date: 2013-10-02, Last modification date: 2023-09-20) |
| 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 Cited by 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: 24055315DOI: 10.1016/j.str.2013.08.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1146 Å) |
Structure validation
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