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The crystal structure of NusB from Mycobacterium tuberculosis

Nature Structural Biology volume 7, pages 475–478 (2000)Cite this article

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.

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Figure 1: Stereo view of the monomer of NusB.
Figure 2: M. tuberculosis NusB is a dimer.
Figure 3: Putative RNA binding motif.
Figure 4: Sequence and structural comparison between NusB homologs.

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Acknowledgements

This work was supported by the Medical Research Council of the UK. We thank S. Gamblin for help in data collection and crystallographic calculations and A. Lane for advice. S. Cole of the Institute Pasteur kindly provided the M. tuberculosis cosmids from which the gene encoding NusB was amplified. This work was supported in part by the European Commission Science Research and Development Programme.

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Authors and Affiliations

  1. Division of Protein Structure, National Institute for Medical Research, London, NW7 1AA, The Ridgeway, Mill Hill, UK

    B. Gopal, Lesley F. Haire, Stephen J. Smerdon & Guy Dodson

  2. Division of Mycobacterial Research, National Institute for Medical Research, London, NW7 1AA, The Ridgeway, Mill Hill, UK

    B. Gopal, Robert A. Cox & M. Jo Colston

  3. Division of Molecular Structure, National Institute for Medical Research, London, NW7 1AA, The Ridgeway, Mill Hill, UK

    Sarah Major

  4. Department of Chemistry, University of York, Y010 5DD, UK

    Jim A. Brannigan & Guy Dodson

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  1. B. Gopal
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Correspondence to Guy Dodson.

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Gopal, B., Haire, L., Cox, R. et al. The crystal structure of NusB from Mycobacterium tuberculosis. Nat Struct Mol Biol 7, 475–478 (2000). https://doi.org/10.1038/75876

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