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Updated: May 7, 2026

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
Published on: November 30, 2018
Crystal structure of Mycobacterium tuberculosis CarD, an essential RNA polymerase binding protein, reveals a
Gundeep Kaur1, Dipak Dutta, Krishan Gopal Thakur
1Structural Biology Laboratory, G. N. Ramachandran Protein Centre, CSIR-Institute of Microbial Technology, Chandigarh, 160036, India.
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.
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