Skip to main content
SpringerLink
Log in

NMR structure note: alkaline proteinase inhibitor APRin from Pseudomonas aeruginosa

  • NMR Structure Note
  • Published:
Journal of Biomolecular NMR Aims and scope Submit manuscript

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
Fig. 3

References

  • Arumugam S, Gray RD, Lane AN (2005) H-1, N-15 and C-13 assignments of the alkaline proteinase inhibitor APRin from Pseudomonas aeruginosa. J Biomol NMR 31:265–266

    Article  Google Scholar 

  • Cavanagh J, Fairbrother WJ, Palmer AG, Skelton AGNJ (1996) Protein NMR spectroscopy principles and practice. Academic Press, San Diego

    Google Scholar 

  • Cornilescu G, Delaglio F, Bax A (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR 13:289–302

    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 6:277–293

    Article  Google Scholar 

  • Dyson HJ, Wright PE (2005) Intrinsically unstructured proteins and their functions. Nature Rev Mol Cell Biol 6:197–208

    Article  Google Scholar 

  • Feltzer RE, Gray RD, Dean WL, Pierce WM (2000) Alkaline proteinase inhibitor of Pseudomonas aeruginosa—interaction of native and N-terminally truncated inhibitor proteins with Pseudomonas metalloproteinases. J Biol Chem 275:21002–21009

    Article  Google Scholar 

  • Feltzer RE, Trent JO, Gray RD (2003) Alkaline proteinase inhibitor of Pseudomonas aeruginosa—a mutational and molecular dynamics study of the role of N-terminal residues in the inhibition of Pseudomonas alkaline proteinase. J Biol Chem 278:25952–25957

    Article  Google Scholar 

  • Gray RD, Trent JO (2005) Contribution of a single-turn alpha-helix to the conformational stability and activity of the alkaline proteinase inhibitor of Pseudomonas aeruginosa. Biochemistry 44:2469–2477

    Article  Google Scholar 

  • Hall JB, Fushman D (2006) Variability of the N-15 chemical shielding tensors in the B3 domain of protein G from N-15 relaxation measurements at several fields. Implications for backbone order parameters. J Am Chem Soc 128:7855–7870

    Article  Google Scholar 

  • Hege T, Feltzer RE, Gray RD, Baumann U (2001) Crystal structure of a complex between Pseudomonas aeruginosa alkaline protease and its cognate inhibitor—inhibition by a zinc-NH2 coordinative bond. J Biol Chem 276:35087–35092

    Article  Google Scholar 

  • Kay LE, Nicholson LK, Delaglio F, Bax A, Torchia DA (1992) Pulse sequences for removal of the effects of cross-correlation between dipolar and chemical-shift anisotropy relaxation mechanism on the measurement of heteronuclear T1 and T2 values in proteins. J Magn Reson 97:359–375

    Google Scholar 

  • Laskowski RA, Rullmann JAC, MacArthur MW, Kaptein R, Thornton JM (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J Biomol NMR 8:477–486

    Article  Google Scholar 

  • Marley J, Lu M, Bracken C (2001) A method for efficient isotopic labeling of recombinant proteins. J Biomol NMR 20:71–75

    Article  Google Scholar 

  • McIntosh PB, Taylor IA, Frenkiel TA, Smerdon SJ, Lane AN (2000) The influence of DNA binding on the backbone dynamics of the yeast cell-cycle protein Mbp1. J Biomol NMR 16:183–196

    Article  Google Scholar 

  • Morihara K, Homma J (1985) Bacterial enzymes and virulence bacterial enzymes and virulence I. Holder. CRC Press, Boca Raton, pp 41–47

    Google Scholar 

  • Morihara K, Hata Y, Okuda K (2000) Serralysin Zn-metalloproteinases—structure, function, secretion pathway, and pathogenicity. Seikagaku 72:16–25

    Google Scholar 

  • Piotto M, Saudek V, Sklenar V (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J Biomol NMR 2:661–665

    Article  Google Scholar 

  • Ruckert M, Otting G (2000) Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments. J Am Chem Soc 122:7793–7797

    Article  Google Scholar 

  • Schwieters CD, Kuszewski JJ, Clore GM (2006) Using Xplor-NIH for NMR molecular structure determination. Prog NMR Spectrosc 48:47–62

    Article  Google Scholar 

  • Wishart DS, Bigam CG, Holm A, Hodges RS, Sykes BD (1995) H-1, C-13 and N-15 random coil NMR chemical-shifts of the common amino-acids .1. Investigations of nearest-neighbor effects. J Biomol NMR 5:67–81

    Article  Google Scholar 

Download references

Acknowledgements

This work was supported by the Kentucky Challenge for Excellence (to ANL). NMR spectra were recorded at the JG Brown Cancer Center NMR Facility with support from The National Science Foundation EPSCoR grant # EPS−0447479 and the Brown Foundation.

Author information

Authors and Affiliations

  1. J.G. Graham Brown Cancer Center, University of Louisville, Louisville, KY, 40202, USA

    Sengodagounder Arumugam & Andrew N. Lane

  2. Department of Biochemistry and Molecular Biology, University of Louisville, Louisville, KY, 40202, USA

    Robert D. Gray

Authors
  1. Sengodagounder Arumugam
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Robert D. Gray
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Andrew N. Lane
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Andrew N. Lane.

Electronic supplementary material

Below is the link to the electronic supplementary material.

(DOC 1810 kb)

Rights and permissions

Reprints and permissions

About this article

Cite this article

Arumugam, S., Gray, R.D. & Lane, A.N. NMR structure note: alkaline proteinase inhibitor APRin from Pseudomonas aeruginosa . J Biomol NMR 40, 213–217 (2008). https://doi.org/10.1007/s10858-008-9218-6

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10858-008-9218-6

Keywords

Search

Navigation