4KBM

Structure of the Mtb CarD/RNAP Beta subunit B1-B2 domains complex

4KBM の概要

• エントリーDOI: 10.2210/pdb4kbm/pdb
• 関連するPDBエントリー: 4KBJ
• 分子名称: DNA-directed RNA polymerase subunit beta, RNA polymerase-binding transcription factor CarD (3 entities in total)
• 機能のキーワード: 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
• 由来する生物種: Mycobacterium tuberculosis; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64199.68

構造登録者

Gulten, G.,Sacchettini, J.C.,TB Structural Genomics Consortium (TBSGC) (登録日: 2013-04-23, 公開日: 2013-10-02, 最終更新日: 2023-09-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.1146 Å)