4MFR

Crystal structure of Mycobacterium tuberculosis CarD

Summary for 4MFR

• Entry DOI: 10.2210/pdb4mfr/pdb
• Related: 4ILU
• Descriptor: RNA polymerase-binding transcription factor CarD, IODIDE ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: tudor-like domain, five helical bundle, transcriptional regulator, rna polymerase, transcription
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 22359.89

Authors

Kaur, G.,Thakur, K.G. (deposition date: 2013-08-28, release date: 2013-11-06, Last modification date: 2024-05-29)

Primary citation

Kaur, G.,Dutta, D.,Thakur, K.G.
Crystal structure of Mycobacterium tuberculosis CarD, an essential RNA polymerase binding protein, reveals a quasidomain-swapped dimeric structural architecture.
Proteins, 82:879-884, 2014

PubMed Abstract: Mycobacterium tuberculosis (Mtb) CarD is an essential transcriptional regulator that binds RNA polymerase and plays an important role in reprogramming transcription machinery under diverse stress conditions. Here, we report the crystal structure of CarD at 2.3 Å resolution, that represents the first structural description of CarD/CdnL-Like family of proteins. CarD adopts an overall bi-lobed structural architecture where N-terminal domain resembles 'tudor-like' domain and C-terminal domain adopts a novel five helical fold that lacks the predicted leucine zipper structural motif. The structure reveals dimeric state of CarD resulting from β-strand swapping between the N-terminal domains of each individual subunits. The structure provides crucial insights into the possible mode(s) of CarD/RNAP interactions.

PubMed: 24115125
DOI: 10.1002/prot.24419

Experimental method

X-RAY DIFFRACTION (2.5 Å)