The crystal structure of NusB from Mycobacterium tuberculosis View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2000-06

AUTHORS

B. Gopal, Lesley F. Haire, Robert A. Cox, M. Jo Colston, Sarah Major, Jim A. Brannigan, Stephen J. Smerdon, Guy Dodson

ABSTRACT

Both prokaryotes and eukaryotes regulate transcription through mechanisms that suppress termination signals. An antitermination mechanism was first characterized in bacteriophage λ. Bacteria have analogous machinery that regulates ribosomal RNA transcription and employs host factors, called the N-utilizing (where N stands for the phage λ N protein) substances (Nus), NusA, NusB, NusE and NusG. Here we report the crystal structure of NusB from Mycobacterium tuberculosis, the bacterium that causes tuberculosis in humans. This molecule shares a similar tertiary structure with the related Escherichia coli protein but adopts a different quaternary organization. We show that, unlike the E. coli homolog, M. tuberculosis NusB is dimeric both in solution and in the crystal. These data help provide a framework for understanding the structural and biological function of NusB in the prokaryotic transcriptional antitermination complex. More... »

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsb0600_475

DOI

http://dx.doi.org/10.1038/nsb0600_475

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1092592903


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