Skip to main content

Advertisement

SpringerLink
Log in

Chemical shift assignments for Rv0577, a putative glyoxylase associated with virulence from Mycobacterium tuberculosis

  • Article
  • Published:
Biomolecular NMR Assignments Aims and scope Submit manuscript

Abstract

Approximately one-third of mankind has been exposed to Mycobacterium tuberculosis, the etiological agent responsible for tuberculosis (TB). As part of an effort to develop a new generation of anti-TB agents, the chemical shifts for the 261-residue, virulence-associated protein Rv0577 from M. tuberculosis has been extensively assigned.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2

Similar content being viewed by others

References

  • Andreu N, Soto CY, Roca I, Martin C, Gibert I (2004) Mycobacterium smegmatis displays the Mycobacterium tuberculosis virulence-related neutral red character when expressing the Rv0577 gene. FEMS Microbiol 231:283–289

    Article  Google Scholar 

  • Buchko GW, Kim C-Y, Terwilliger TC, Kennedy MA (2006) Solution structure of the conserved hypothetical protein Rv2302 from Mycobacterium tuberculosis. J Bacteriol 188:5993–6001

    Article  Google Scholar 

  • Enarson DA (2003) Tuberculosis as a global public health problem. In: Kaufmann SHE, Hahn H (eds) Mycobacteria and TB. Kargel, Basel, pp 1–16

    Google Scholar 

  • Myler PJ, Stacy R, Stewart LJ, Staker BL, Van Voorhis WC, Varani G, Buchko GW (2009) The Seattle Structural Genomics Center for Infectious Disease (SSGCID). Infect Diseases Drug Targets 9:493–506

    Article  Google Scholar 

  • Pethe K, Sequeira PC, Agarwalla S, Rhee K, Kuhen K, Phong WY, Patel V, Beer D, Walker JR, Duraiswamy J, Jiricek J, Keller TH, Chatterjee A, Tan MP, Ujjini M, Rao SPS, Camacho L, Bifani P, Mak PA, Ma I, Barnes SW, Chen Z, Plouffe D, Thayalan P, Ng SH, Au M, Lee BH, Tan BH, Ravindran S, Nanjundappa M, Lin X, Goh A, Lakshminarayana SB, Shoen C, Cynamon M, Kreiswirth B, Dartois V, Peters EC, Glynne R, Brenner S, Dick T (2010) A chemical genetic screen in Mycobacterium tuberculosis identifies carbon-source-dependent growth inhibitors devoid of in vivo efficiency. Nature Comm 1:57

    ADS  Google Scholar 

  • Russell DG, Barry CE III, Flynn JL (2010) Tuberculosis: what we don’t know can, and does, hurt us. Science 328:852–856

    Article  ADS  Google Scholar 

  • Szyperski T, Yeh DC, Sukumaran DK, Moseley HNB, Montelione GT (2002) Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment. Proc Natl Acad Sci USA 99:8009–8014

    Article  ADS  Google Scholar 

  • Wishart DS, Sykes BD (1994) The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 4:171–180

    Article  Google Scholar 

  • World Health Organization (2009) Globular tuberculosis control: a short update to the 2009 report. Geneva

  • Zuiderweg ERP (2002) Mapping protein–protein interactions in solution using NMR spectroscopy. Biochemistry 41:1–7

    Article  Google Scholar 

Download references

Acknowledgments

Funding for this research was provided by the National Institute of Allergy and Infectious Diseases, National Institute of Health, Department of Health and Human Services, under Federal Contract number HHSN272200700057C. The SSGCID internal ID for Rv0577 is MytuD.17269.a. Much of this research was performed at the W.R. Wiley Environmental Molecular Sciences Laboratory (EMSL), a national scientific user facility located at Pacific Northwest National Laboratory (PNNL) and sponsored by US Department of Energy’s Office of Biological and Environmental Research (BER) program. Battelle operates PNNL for the US Department of Energy.

Author information

Authors and Affiliations

  1. Biological Sciences Division and Seattle Structural Genomics Center for Infectious Disease, Pacific Northwest National Laboratory, Richland, WA, 99352, USA

    Garry W. Buchko

  2. Bioscience Division, Los Alamos National Laboratory, Los Alamos, NM, 87545, USA

    Heungbok Kim, Thomas C. Terwilliger & Chang-Yub Kim

  3. Seattle Biomedical Research Institute and Seattle Structural Genomics Center for Infectious Disease, Seattle, WA, 98109-5219, USA

    Peter J. Myler

  4. Department of Medical Education and Biomedical Informatics, University of Washington, Seattle, WA, 98195, USA

    Peter J. Myler

  5. Department of Global Health, University of Washington, Seattle, WA, 98195, USA

    Peter J. Myler

Authors
  1. Garry W. Buchko
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Heungbok Kim
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Peter J. Myler
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Thomas C. Terwilliger
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Chang-Yub Kim
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding authors

Correspondence to Garry W. Buchko or Chang-Yub Kim.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Buchko, G.W., Kim, H., Myler, P.J. et al. Chemical shift assignments for Rv0577, a putative glyoxylase associated with virulence from Mycobacterium tuberculosis . Biomol NMR Assign 6, 43–46 (2012). https://doi.org/10.1007/s12104-011-9322-5

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12104-011-9322-5

Keywords

Search

Navigation