Skip to main content

Backbone and sterospecific methyl side chain resonance assignments of the homodimeric zinc sensor AdcR (32 kDa) in the apo- and Zn(II)-bound states


Streptococcus pneumoniae adhesin competence repressor (AdcR) is a Zn(II)-dependent 32 kDa homodimer that controls the transcription of a zinc-specific ABC uptake system (AdcABC), three pneumococcal histidine triad proteins (PhtA, PhtD and PhtE), and an AdcA homolog AdcAII. AdcR is the first metal-dependent member of the MarR family of prokaryotic transcriptional repressors. Two-dimensional NMR studies reveal large changes in the spectrum upon Zn(II) binding. Near complete backbone and stereospecific methyl group resonance assignments for apo- and Zn(II)-AdcR are presented here.

This is a preview of subscription content, access via your institution.

Fig. 1
Fig. 2
Fig. 3


  • Bahrami A, Assadi AH, Markley JL, Eghbalnia HR (2009) Probabilistic interaction network of evidence algorithm and its application to complete labeling of peak lists from protein NMR spectroscopy. PLoS Comput Biol 5(3):e1000307

    Article  Google Scholar 

  • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6(3):277–293

    Article  Google Scholar 

  • Guerra AJ, Dann CE III, Giedroc DP (2011) Crystal structure of the zinc-dependent MarR family transcriptional regulator AdcR in the Zn(II)-bound state. J Am Chem Soc 133(49):19614–19617

    Article  Google Scholar 

  • Hava DL, Camilli A (2002) Large-scale identification of serotype 4 Streptococcus pneumoniae virulence factors. Mol Microbiol 45(5):1389–1406

    Google Scholar 

  • Hilty C, Wider G, Fernandez C, Wuthrich K (2003) Stereospecific assignments of the isopropyl methyl groups of the membrane protein OmpX in DHPC micelles. J Biomol NMR 27(4):377–382

    Article  Google Scholar 

  • Kay L, Keifer P, Saarinen T (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J Am Chem Soc 114(26):10663–10665

    Article  Google Scholar 

  • Reyes-Caballero H, Guerra AJ, Jacobsen FE, Kazmierczak KM, Cowart D, Koppolu UM, Scott RA, Winkler ME, Giedroc DP (2010) The metalloregulatory zinc site in Streptococcus pneumoniae AdcR, a zinc-activated MarR family repressor. J Mol Biol 403(2):197–216

    Article  Google Scholar 

  • Tugarinov V, Kay LE (2003) Ile, Leu, and Val methyl assignments of the 723-residue malate synthase G using a new labeling strategy and novel NMR methods. J Am Chem Soc 125(45):13868–13878

    Article  Google Scholar 

  • Waugh DS (1996) Genetic tools for selective labeling of proteins with alpha-15 N-amino acids. J Biomol NMR 8(2):184–192

    Article  Google Scholar 

  • Yamazaki T, Lee W, Arrowsmith CH, Muhandiram DR, Kay LE (1994) A suite of triple resonance NMR experiments for the backbone assignment of 15 N, 13C, 2H labeled proteins with high sensitivity. J Am Chem Soc 116(26):11655–11666

    Article  Google Scholar 

Download references


This work was supported by the NIH grant GM042569 (to D.P.G.).

Conflict of interest

The authors declare that they have no conflict of interest.

Author information

Authors and Affiliations


Corresponding author

Correspondence to David P. Giedroc.

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Guerra, A.J., Giedroc, D.P. Backbone and sterospecific methyl side chain resonance assignments of the homodimeric zinc sensor AdcR (32 kDa) in the apo- and Zn(II)-bound states. Biomol NMR Assign 8, 11–14 (2014).

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI:


  • Metalloregulatory protein
  • Winged helix
  • Zinc sensor
  • Allosteric regulation
  • S. pneumoniae