Advertisement

Biomolecular NMR Assignments

, Volume 1, Issue 2, pp 209–211 | Cite as

Main chain NMR assignments of subtilisin Sbt70 in its prodomain-bound state

  • Nese Sari
  • Kathryn E. Fisher
  • Philip N. Bryan
  • John OrbanEmail author
Article

Abstract

Main chain assignments are described for a 266-residue subtilisin mutant, Sbt70, in its 35 kDa complex with an N-terminal prodomain. The assignments provide the basis for understanding how the prodomain assists folding of subtilisin at a residue-specific level.

Keywords

Subtilisin Prodomain NMR Folding 

Notes

Acknowledgments

This work was supported by NIH Grants GM42560, 1S10RR15744, and the W. M. Keck Foundation.

References

  1. Bryan PN (2002) Prodomains and protein folding catalysis. Chem Rev 102:4805–4816CrossRefGoogle Scholar
  2. Bryan P, Wang L, Hoskins J, Ruvinov S, Strausberg S, Alexander P, Almog O, Gilliland G, Gallagher TD (1995) Catalysis of a protein folding reaction: mechanistic implications of the 2.0 Å structure of the subtilisin-prodomain complex. Biochemistry 34:10310–10318CrossRefGoogle Scholar
  3. 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 6:277–293CrossRefGoogle Scholar
  4. Fisher KE, Ruan B, Alexander PA, Wang L, Bryan PN (2007) Mechanism of the kinetically-controlled folding reaction of subtilisin. Biochemistry 46:640–651CrossRefGoogle Scholar
  5. Fogh RH, Schipper D, Boelens R, Kaptein R (1994) 1H, 13C and 15N NMR backbone assignments of the 269-residue serine protease PB92 from Bacillus alcalophilus. J Biomol NMR 4:123–128CrossRefGoogle Scholar
  6. Fogh RH, Schipper D, Boelens R, Kaptein R (1995) Complete 1H, 13C and 15N NMR assignments and secondary structure of the 269-residue serine protease PB92 from Bacillus alcalophilus. J Biomol NMR 5:259–270CrossRefGoogle Scholar
  7. Goddard TD, Kneller DG SPARKY, University of California San FranciscoGoogle Scholar
  8. Remerowski ML, Domke T, Groenewegen A, Pepermans HAM, Hilbers CW, van de Ven FJM (1994) 1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue protease subtilisin 309 from Bacillus lentus. J Biomol NMR 4:257–278CrossRefGoogle Scholar
  9. Ruan B, Hoskins J, Bryan P (1999) Rapid folding of calcium-free subtilisin by a stabilized pro-domain mutant. Biochemistry 38:8562–8571CrossRefGoogle Scholar
  10. Sari N, Ruan B, Fisher KE, Alexander PA, Orban J, Bryan PN (2007) Hydrogen-deuterium exchange in free and prodomain-complexed subtilisin. Biochemistry 46:652–658CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media B.V. 2007

Authors and Affiliations

  • Nese Sari
    • 1
  • Kathryn E. Fisher
    • 1
  • Philip N. Bryan
    • 1
  • John Orban
    • 1
    Email author
  1. 1.Center for Advanced Research in BiotechnologyUniversity of Maryland Biotechnology InstituteRockvilleUSA

Personalised recommendations