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Crystal structure of Mycobacterium tuberculosis CarD, an essential RNA polymerase binding protein, reveals a quasidomain-swapped dimeric structural architecture.

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Crystal structure of Mycobacterium tuberculosis CarD, an essential RNA polymerase binding protein, reveals a quasidomain-swapped dimeric structural architecture.
 
Creator Kaur, Gundeep
Dutta, Dipak
Thakur, Krishan Gopal
 
Description 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.
 
Publisher New York, NY : Wiley-Liss
 
Date 2014-05
 
Type Article
PeerReviewed
 
Relation http://onlinelibrary.wiley.com/doi/10.1002/prot.24419/abstract;jsessionid=CDAC202B58D6CE8D5DF9347F85F19842.f03t03
http://crdd.osdd.net/open/1572/
 
Identifier Kaur, Gundeep and Dutta, Dipak and Thakur, Krishan Gopal (2014) Crystal structure of Mycobacterium tuberculosis CarD, an essential RNA polymerase binding protein, reveals a quasidomain-swapped dimeric structural architecture. Proteins, 82 (5). pp. 879-84. ISSN 1097-0134